Information on EC 1.18.1.2 - ferredoxin-NADP+ reductase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
1.18.1.2
-
RECOMMENDED NAME
GeneOntology No.
ferredoxin-NADP+ reductase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
interaction between ferredoxin and ferredoxin-NADP+ reductase
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
catalytic mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
catalytic mechanism, initiated by reduction of FAD cofactor by obligatory one-electron carriers ferredoxin or flavodoxin in presence of NADP+, the enzymes' C-terminal tyrosine residue is involved modulating the enzyme affinity for NADP+/NADPH
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
ping pong bi bi mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
catalytic mechanism of forward and reverse reactions
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
Glu139 is essential for interaction with the substrate steering ferredoxin, flavodoxin and NADP+/NADPH in appropriate position for docking, Glu139 is not involved in binding
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism, interaction and electron transfer
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
active site structure, reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
active site structure of the plant-type enzyme, reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism, substrate recognition mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
active site structure, reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
active site structure, ping pong reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
active site structure, reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
coenzyme recognition and reaction mechanism
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
mechanism of coenzyme recognition and binding
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism via semiquinone intermediate and radical formation, enzyme-substrate interactions, overview
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism via semiquinone intermediate and radical formation
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction mechanism via semiquinone intermediate and radical formation, enzyme-substrate interactions, overview
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
reaction and substrate binding mechanism, in vivo catalytic cycle
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
positively charged residues K83 and K89 are required for catalytic activity, methylation of K83, K89, and K135 is required for optimal enzyme activity
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
hydride transfer between Anabaena FNR and NADP+/H occurs through formation of two charge transfer complexes. FNR and NADP+/H conformations and orientation during the enzyme:coenzyme interaction is critical during formation of charge transfer complexes, which are necessary for an efficient hydride transfer
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
hydride exchange occurs at 30-150 per s being not limiting for enzyme activity. Electron transfer to flavodoxin proceeds at 2.7 per s, in the range of steady-state catalysis, supporting that flavodoxin oscillates between the semiquinone and fully reduced states when enzyme operates in vivo
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
FNR is able to transfer electrons between one-electron carriers, ferredoxin or flavodoxin, and two-electron carriers, NADP+ and NADPH, involving its redox cofactor FAD, involvement of Glu312 in the FNR catalytic mechanism not only as a proton donor but also as a key residue for stabilizing and destabilizing reaction intermediates, reaction mechanism and catalytic cycle, overview
-
2 reduced ferredoxin + NADP+ + H+ = 2 oxidized ferredoxin + NADPH
show the reaction diagram
catalytic mechanism of forward and reverse reactions
Anabaena sp. PCC7119
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
Photosynthesis
-
photosynthesis light reactions
-
ubiquinol-6 biosynthesis from 4-aminobenzoate (eukaryotic)
-
SYSTEMATIC NAME
IUBMB Comments
ferredoxin:NADP+ oxidoreductase
A flavoprotein (FAD). In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe-2S] ferredoxins, but in other bacteria it can also reduce bacterial [4Fe-4S] ferredoxins and flavodoxin.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
adrenodoxin reductase
-
-
-
-
adrenodoxin reductase
-
-
AnFNR
-
FNR from Anabaena PCC 7119
cytochrome b6f -associated ferredoxin:NADP+ oxidoreductase
-
-
DA1
-
-
-
-
EC 1.6.7.1
-
-
formerly
-
EC 1.6.99.4
-
-
formerly
-
Fd-NADP+ reductase
-
-
Fd-NADP+ reductase
Chlorobaculum tepidum CT1512
-
-
-
Fd-NADP+ reductase
-
-
Fd-NADP+ reductase
-
-
Fd-NADP+ reductase
-
-
ferredoxin (flavodoxin)-(reduced) nicotinamide adenine dinucleotide phosphate reductase
Q9L6V3
-
ferredoxin (flavodoxin)-(reduced) nicotinamide adenine dinucleotide phosphate reductase
Rhodobacter capsulatus 37b4
Q9L6V3
-
-
ferredoxin (flavodoxin)-NADP(H) reductase
-
-
ferredoxin (flavodoxin)-NADP(H) reductase
Anabaena sp. PCC7119
-
-
-
ferredoxin (flavodoxin)-NADP(H) reductase
Q9L6V3
-
ferredoxin (flavodoxin)-NADP(H) reductase
Rhodobacter capsulatus 37b4
Q9L6V3
-
-
ferredoxin (flavodoxin)-NADP(H) reductase
-
-
ferredoxin (flavodoxin):NADP+ oxidoreductase
-
-
ferredoxin NADP reductase
-
-
ferredoxin NADP+ oxidoreductase
Q8RVZ8, Q8RVZ9
-
ferredoxin NADP+ oxidoreductase
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
ferredoxin NADP+ reductase
-
-
ferredoxin nicotinamide adenine dinucleotide phosphate reductase
-
-
ferredoxin-NADP oxidoreductase
-
-
-
-
ferredoxin-NADP reductase
-
-
-
-
ferredoxin-NADP reductase
-
-
Ferredoxin-NADP(+) reductase
-
-
-
-
Ferredoxin-NADP(+) reductase
-
-
Ferredoxin-NADP(+) reductase
Chlorobaculum tepidum CT1512
-
-
-
Ferredoxin-NADP(+) reductase
-
-
Ferredoxin-NADP(+) reductase
-
-
ferredoxin-NADP(H) oxidoreductase
-
-
ferredoxin-NADP(H) reductase
-
-
ferredoxin-NADP(H) reductase
Anabaena sp. PCC7119
-
-
-
ferredoxin-NADP(H) reductase
-
-
ferredoxin-NADP(H) reductase
-
-
ferredoxin-NADP(H) reductase
-
-
ferredoxin-NADP(H) reductase
-
-
ferredoxin-NADP+ oxidoreductase
F4JZ46
-
ferredoxin-NADP+ oxidoreductase
Q8W493
-
ferredoxin-NADP+ oxidoreductase
Q9FKW6
-
ferredoxin-NADP+ oxidoreductase
-
-
ferredoxin-NADP+ oxidoreductase
Arthrospira platensis IAM M-135
-
-
-
ferredoxin-NADP+ oxidoreductase
-
-
ferredoxin-NADP+ oxidoreductase
O05268
-
ferredoxin-NADP+ oxidoreductase
-
-
ferredoxin-NADP+ oxidoreductase
Q93RE3
-
ferredoxin-NADP+ oxidoreductase
-
-
ferredoxin-NADP+ oxidoreductase
Synechocystis sp. 6803
-
-
-
ferredoxin-NADP+ oxidoreductase
Q8RVZ8, Q8RVZ9
-
ferredoxin-NADP+ oxidoreductase
Q9SLP6
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
P28861
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+ reductase
-
-
ferredoxin-NADP+-oxidoreductase
Q8W493, Q9FKW6
-
ferredoxin-NADP+-reductase
-
-
ferredoxin-NADP-oxidoreductase
-
-
-
-
ferredoxin-NADP-reductase
-
-
ferredoxin-nicotinamide adenine dinucleotide phosphate reductase
-
-
ferredoxin-nicotinamide-adenine dinucleotide phosphate (oxidized) reductase
-
-
-
-
ferredoxin-TPN reductase
-
-
-
-
ferredoxin:NADP(+) oxidoreductase
-
-
ferredoxin:NADP(+) oxidoreductase
Q8RVZ8, Q8RVZ9
-
ferredoxin:NADP+ oxidoreductase
-
-
-
-
ferredoxin:NADP+ oxidoreductase
-
-
ferredoxin:NADP+ oxidoreductase
-
-
ferredoxin:NADP+ reductase
Q5CVU8
-
ferredoxin:NADP+ reductase
Cryptosporidium parvum IOWA-1
Q5CVU8
-
-
ferredoxin:NADPH oxidoreductase
-
-
ferric reductase
P28861
-
Flavodoxin reductase
-
-
-
-
FLDR
-
-
-
-
FLXR
-
-
-
-
FNR
-
-
-
-
FNR
Anabaena sp. PCC7119
-
-
-
FNR
Arthrospira platensis IAM M-135
-
-
-
FNR
O05268
-
FNR
Chlorobaculum tepidum CT1512
-
-
-
FNR
Synechocystis sp. 6803
-
-
-
FNR
Q8RVZ8, Q8RVZ9
-
FNR
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
FNR
Q9SLP6
-
FNR-A
Q8RVZ9
isozyme
FNR-B
Q8RVZ8
isozyme
FNR1
Q9FKW6
In Arabidopsis thaliana, two distinct chloroplast-targeted FNR isoforms, FNR1 and FNR2, are encoded by nuclear genes At5g66190 and At1g20020, respectively. In wild-type plants, both FNR isoforms exist partially in soluble form in the stroma and partially attached to the thylakoid membrane, as well as to the inner envelope membrane of the chloroplast.
FNR2
Q8W493
In Arabidopsis thaliana, two distinct chloroplast-targeted FNR isoforms, FNR1 and FNR2, are encoded by nuclear genes At5g66190 and At1g20020, respectively. In wild-type plants, both FNR isoforms exist partially in soluble form in the stroma and partially attached to the thylakoid membrane, as well as to the inner envelope membrane of the chloroplast.
FPR
P28861
-
FPR
Rhodobacter capsulatus 37b4
Q9L6V3
-
-
FprA
-
Pseudomonas putida harbors two ferredoxin-NADP+ reductases FprA and FprB on its chromosome.
FprB
-
Pseudomonas putida harbors two ferredoxin-NADP+ reductases FprA and FprB on its chromosome.
LFNR1
Q9FKW6
isozyme, involved in linear electron transfer and thereby affects the function of the Calvin cycle
LFNR2
Q8W493
isozyme
mitochondrial-type ferredoxin:NADP+ reductase
Q5CVU8
-
mtFNR
Cryptosporidium parvum IOWA-1
Q5CVU8
-
-
NADP:ferredoxin oxidoreductase
-
-
-
-
NADPH ferredoxin reductase
-
-
NADPH-dependent ferredoxin reductase
-
-
NADPH:ferredoxin oxidoreductase
-
-
-
-
NFR
-
-
-
-
PfFNR
-
ferredoxin-NADP+ reductase of Plasmodium falciparum
pFNR
Q8RVZ8, Q8RVZ9
-
pFNR
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
photosynthetic ferredoxin NADP+ oxidoreductase
Q8RVZ8, Q8RVZ9
-
photosynthetic ferredoxin NADP+ oxidoreductase
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
photosynthetic FNR
Q8RVZ8, Q8RVZ9
-
photosynthetic FNR
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
reduced nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase
-
-
-
-
reductase, ferredoxin-nicotinamide adenine dinucleotide phosphate
-
-
-
-
ST2133
Q96YN9
locus name
ST2133
Sulfolobus tokodaii 7
Q96YN9
locus name
-
TPNH-ferredoxin reductase
-
-
-
-
mitochondrial-type ferredoxin:NADP+ reductase
Cryptosporidium parvum IOWA-1
Q5CVU8
-
-
additional information
-
enzyme belongs to the plant-type enzyme family
additional information
Anabaena sp. PCC7119
-
enzyme belongs to the plant-type enzyme family
-
additional information
-
leaf-type, or chloroplast, or photosynthetic LFNR
additional information
-
enzyme belongs to the bacterial-type enzyme family
additional information
-
enzyme belongs to the plant-type enzyme family
additional information
-
enzyme belongs more to the plant-type enzyme family than to the bacterial-type enzyme family
additional information
-
enzyme belongs to the bacterial-type enzyme family
additional information
-
enzyme belongs to the plant-type enzyme family, result of lateral gene transfer
additional information
-
leaf-type, or chloroplast, or photosynthetic LFNR
additional information
-
formerly termed thylakoid-bound diaphorase
additional information
-
enzyme belongs to the plant-type enzyme family
additional information
-
leaf-type, or chloroplast, or photosynthetic LFNR
CAS REGISTRY NUMBER
COMMENTARY
56367-57-8
-
9029-33-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
cyanobacterium
-
-
Manually annotated by BRENDA team
PCC 7119
-
-
Manually annotated by BRENDA team
PCC 7119
Uniprot
Manually annotated by BRENDA team
PCC7119
-
-
Manually annotated by BRENDA team
petH gene product
-
-
Manually annotated by BRENDA team
strain 7119, multiple forms: FNR-I, FNR-II, FNR-III, FNR-IV
-
-
Manually annotated by BRENDA team
strain PCC 7119
-
-
Manually annotated by BRENDA team
strain PCC7119
-
-
Manually annotated by BRENDA team
Anabaena sp. 7119
strain 7119, multiple forms: FNR-I, FNR-II, FNR-III, FNR-IV
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC7119
PCC7119
-
-
Manually annotated by BRENDA team
Anabaena sp. PCC7119
strain PCC7119
-
-
Manually annotated by BRENDA team
cyanobacterium
-
-
Manually annotated by BRENDA team
ecotype Columbia
UniProt
Manually annotated by BRENDA team
isozyme FNRI; plastidic isozyme FNRI, gene FNR2
UniProt
Manually annotated by BRENDA team
isozyme FNRII; plastidic isozyme FNRII, gene FNR1
UniProt
Manually annotated by BRENDA team
two LFNR isoforms, LFNR1 and LFNR2
-
-
Manually annotated by BRENDA team
wild type and T-DNA insertion line fnr1 (lacking FNR1) and RNAi line fnr2 (lacking FNR2)
UniProt
Manually annotated by BRENDA team
2 forms: FNRS I and FNRS II
-
-
Manually annotated by BRENDA team
strain IAM M-135, cyanobacterium
-
-
Manually annotated by BRENDA team
Arthrospira platensis IAM M-135
strain IAM M-135, cyanobacterium
-
-
Manually annotated by BRENDA team
gene yumC
UniProt
Manually annotated by BRENDA team
marine green algae
-
-
Manually annotated by BRENDA team
xanthophycean algae
-
-
Manually annotated by BRENDA team
paprika
Uniprot
Manually annotated by BRENDA team
strain CT1512
-
-
Manually annotated by BRENDA team
Chlorobaculum tepidum CT1512
strain CT1512
-
-
Manually annotated by BRENDA team
single copy FNR
UniProt
Manually annotated by BRENDA team
Cryptosporidium parvum IOWA-1
single copy FNR
UniProt
Manually annotated by BRENDA team
strain RK-1, red alga
Uniprot
Manually annotated by BRENDA team
Cyanidium caldarium RK-1
strain RK-1, red alga
Uniprot
Manually annotated by BRENDA team
chick
-
-
Manually annotated by BRENDA team
parasitic bacterium
-
-
Manually annotated by BRENDA team
cyanobacterium strain 7119
-
-
Manually annotated by BRENDA team
strain MAC, cyanobacterium
-
-
Manually annotated by BRENDA team
strain MAC, cyanobacterium
-
-
Manually annotated by BRENDA team
expression in Nicotiana tabacum
-
-
Manually annotated by BRENDA team
multiple isoenzymes
-
-
Manually annotated by BRENDA team
strain KT2440
-
-
Manually annotated by BRENDA team
strain KT2440, wild type and mutants
-
-
Manually annotated by BRENDA team
strain KT2440, wild type and mutants fprA (lacking FprA) and fprB (lacking FprB)
-
-
Manually annotated by BRENDA team
radish, var acanthiformis cultivar miyashige
-
-
Manually annotated by BRENDA team
Wistar, male, H18H
-
-
Manually annotated by BRENDA team
strain 37b4
SwissProt
Manually annotated by BRENDA team
Rhodobacter capsulatus 37b4
strain 37b4
SwissProt
Manually annotated by BRENDA team
induction by treatment of worms with reactive oxygen species generating compounds
Uniprot
Manually annotated by BRENDA team
2 FNR isozymes
-
-
Manually annotated by BRENDA team
2 forms: P-1, P-2
-
-
Manually annotated by BRENDA team
2 tissue-specific isozymes in leaf and root
-
-
Manually annotated by BRENDA team
5 molecular forms: a, b, c, d, e
-
-
Manually annotated by BRENDA team
6 different forms differ in specific activities in various assay systems and affinity for NADPH, interconvertible at 4C
-
-
Manually annotated by BRENDA team
ferredoxin NADP reductase binding protein is not related to CF0II
-
-
Manually annotated by BRENDA team
spinach, multiple forms
-
-
Manually annotated by BRENDA team
strain Atlanta
-
-
Manually annotated by BRENDA team
Spinacia oleracea Atlanta
strain Atlanta
-
-
Manually annotated by BRENDA team
blue-green algae
-
-
Manually annotated by BRENDA team
Sulfolobus tokodaii 7
-
SwissProt
Manually annotated by BRENDA team
i.e. Thermosynechococcus elongatus, single copy gene petH
SwissProt
Manually annotated by BRENDA team
strain PCC 7002, gene petH
-
-
Manually annotated by BRENDA team
thermophilic blue-green algae
-
-
Manually annotated by BRENDA team
PCC6803, gene petH
-
-
Manually annotated by BRENDA team
strain PCC6803, two isoforms of enzyme, produced from the same gene via an internal ribosome entry site within the ORF. Isoform FNRS specifically accumulates under heterotrophic conditions, isoform FNRL contains an N-terminal domain that allows its association with the phycobilisome
SwissProt
Manually annotated by BRENDA team
Synechocystis sp. 6803
-
-
-
Manually annotated by BRENDA team
Synechocystis sp. PCC6803
strain PCC6803, two isoforms of enzyme, produced from the same gene via an internal ribosome entry site within the ORF. Isoform FNRS specifically accumulates under heterotrophic conditions, isoform FNRL contains an N-terminal domain that allows its association with the phycobilisome
SwissProt
Manually annotated by BRENDA team
isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS; four photosynthetic pFNR protein isoforms
UniProt
Manually annotated by BRENDA team
isozyme FNRI; isozyme FNRI, gene FNRI or FNR-B
UniProt
Manually annotated by BRENDA team
isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD; four photosynthetic pFNR protein isoforms
UniProt
Manually annotated by BRENDA team
isozyme FNRII; isozyme FNRII, gene FNRII
UniProt
Manually annotated by BRENDA team
Triticum aestivum Paragon
isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS; four photosynthetic pFNR protein isoforms
UniProt
Manually annotated by BRENDA team
Triticum aestivum Paragon
isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD; four photosynthetic pFNR protein isoforms
UniProt
Manually annotated by BRENDA team
corn root
-
-
Manually annotated by BRENDA team
isozyme FNRII; isozyme FNRII, gene L-FNRII or FNR2; isozyme FNRI; isozyme FNRI, gene L-FNRI or FNR1
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
metabolism
-
function in ferric iron metabolism
metabolism
Q8W493, Q9FKW6
FNR mediates the final step of photosynthetic electron flow by transferring electrons from ferredoxin to NADP+; FNR mediates the final step of photosynthetic electron flow by transferring electrons from ferredoxin to NADP+
metabolism
F4JZ46, Q8W493
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways; FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
metabolism
Q8RVZ8, Q8RVZ9
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways; FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
metabolism
Q9SLP6
FNR catalyzes the last step of the linear electron transfer chain in chloroplasts. But FNR also functions in the crossing of various electron transfer pathways
physiological function
-
FNR mediates the redox reaction between NADP+/NADPH and ferredoxin, providing redox equivalents in cell-material synthesis
physiological function
-
ferredoxin and Fd-NADP+ reductase are redox partners responsible for the conversion between NADP+ and NADPH in the plastids of photosynthetic organisms
physiological function
Q8RVZ8, Q8RVZ9
the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview; the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview
physiological function
-
in chloroplasts and cyanobacteria, FNR provides the NADPH necessary for photosynthetic CO2 assimilation
physiological function
-
FNR catalyzes the final step of the linear photosynthetic electron flow by mediating the electron transfer from reduced ferredoxin to NADP+ with formation of NADPH for CO2 assimilation or other biosynthetic pathways. This process is a rate-limiting step of photosynthesis under both limiting and saturating light conditions. FNR is also involved in the cyclic electron flow around photosystem I, cyclic PSI, by its photoproduct NADPH recycling to plastoquinone or the cytochrome b6f complex. Analysis of contribution of FNR and NDH-1 to cyclic PSI under low CO2 conditions, overview
physiological function
-
FNR associated with the cytochrome b6f complex can participate in the cyclic electron transport as photosystem I-plastoquinone or NADPH-plastoquinone oxidoreductase
physiological function
-
FNR catalyses the ferredoxin-dependent reduction of NADP+ to NADPH in linear photosynthetic electron transport. The enzyme also transfers electrons from reduced ferredoxin or NADPH to the cytochrome b6f complex in cyclic electron transport
physiological function
-, Q5CVU8
in the photosystem I, an oxidized ferredoxin molecule, Fdox, first receives an electron driven by light energy to form a reduced ferredoxin, Fdred. The FAD-containing FNR then catalyzes the transfer of the electron to NADP+, which recycles Fdred back to Fdox. On the other hand, FNR mainly catalyzes the conversion from Fdox to Fdred in reactions other than photosynthesis
physiological function
-
the ferredoxin:ferredoxin-NADP+ oxidoreductase couple is an important mediator for these processes because it provides the transition from exclusively membrane-bound light reactions to the mostly stromal metabolic pathways
physiological function
Cryptosporidium parvum IOWA-1
-
in the photosystem I, an oxidized ferredoxin molecule, Fdox, first receives an electron driven by light energy to form a reduced ferredoxin, Fdred. The FAD-containing FNR then catalyzes the transfer of the electron to NADP+, which recycles Fdred back to Fdox. On the other hand, FNR mainly catalyzes the conversion from Fdox to Fdred in reactions other than photosynthesis
-
physiological function
Synechocystis sp. 6803
-
FNR catalyzes the final step of the linear photosynthetic electron flow by mediating the electron transfer from reduced ferredoxin to NADP+ with formation of NADPH for CO2 assimilation or other biosynthetic pathways. This process is a rate-limiting step of photosynthesis under both limiting and saturating light conditions. FNR is also involved in the cyclic electron flow around photosystem I, cyclic PSI, by its photoproduct NADPH recycling to plastoquinone or the cytochrome b6f complex. Analysis of contribution of FNR and NDH-1 to cyclic PSI under low CO2 conditions, overview
-
physiological function
Triticum aestivum Paragon
-
the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview; the photosynthetic FNRs may be crucial to the regulation of reductant partition between carbon fixation and other metabolic pathways. The alternative N-terminal pFNRI and pFNRII protein isoforms have statistically significant differences in response to the physiological parameters of chloroplast maturity, nitrogen regime, and oxidative stress, overview
-
metabolism
P28861
the enzyme also drives the Fenton reaction
additional information
-
introduction of specific disulfide bonds between ferredoxin and Fd-NADP+ reductase by engineering cysteines into the two proteins results in 13 different Fd-FNR cross-linked complexes displaying a broad range of activity to catalyze the NADPH-dependent cytochrome c reduction
additional information
-
while in the wild-type, vibrational enhanced modulation of the active site contributes to the tunnel probability of hydride transfer, complexes of some of the active site mutants with the coenzyme hardly allow the relative movement of isoalloxazine and nicotinamide rings along the hydride transfer reaction. The architecture of the wild-type FNR active site precisely contributes to reduce the stacking probability between the isoalloxazine and nicotinamide rings in the catalytically competent complex, modulating the angle and distance between the N5 of the FAD isoalloxazine and the C4 of the coenzyme nicotinamide to values that ensure efficient hydride transfer processes
additional information
F4JZ46, Q8W493
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery; chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants. Inactivation of one chloroplast FNR isoform does not result in upregulation of the expression of the other isozyme, neither at the level of transcription nor translation, but results in general downregulation of the photosynthetic machinery
additional information
Q8RVZ8, Q8RVZ9
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants; chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants
additional information
Q9SLP6
chloroplast proteins Tic62 and TROL anchor the enzyme to the thylokoid membrane. Tic62-FNR complexes are not directly involved in photosynthetic reactions, but Tic62 protects FNR from inactivation during the dark periods. TROL-FNR complexes have an impact on the photosynthetic performance of the plants
additional information
-
titration behaviour of Glu312, overview
additional information
-
FNR interacts with Tic62, a member of the Tic complex, i.e. translocon at the inner envelope of chloroplasts, involved in redox-regulation of protein import into chloroplasts. Tic62 represents a major FNR interaction protein partner at the thylakoids, and binding to Tic62 clearly increases the stability of FNR. The specific interaction with FNR is mediated by a conserved sequence motif rich in proline and serine residues, located in the C terminus of Tic62
additional information
-
the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast. In Arabidopsis mutants completely devoid of FNR1 or FNR2 all high molecular weight FNR complexes are absent
additional information
-
the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast. Nicotiana tabacum mutants with inactivated ndh genes show no reduction in the accumulation of FNR at the thylakoid membrane
additional information
-
the correct distribution of FNR between stroma and thylakoids is used to efficiently regulate ferredoxin-dependent electron partitioning in the chloroplast
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,4-benzoquinone + NADP+
? + NADPH + H+
show the reaction diagram
Anabaena sp., Anabaena sp. PCC7119
-
single electron reduction potential 0.09 V
-
-
?
1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
Anabaena sp., Anabaena sp. PCC7119
-
single electron reduction potential -0.15 V
-
-
?
1,8-dihydroxy-9,10-anthraquinone + NADP+
? + NADPH + H+
show the reaction diagram
Anabaena sp., Anabaena sp. PCC7119
-
single electron reduction potential -0.325 V
-
-
?
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q8RVZ8, Q8RVZ9
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q8RVZ8, Q8RVZ9
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
F4JZ46, Q8W493
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-, Q5CVU8
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
O05268
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q9SLP6
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-, Q5CVU8
cyt c-coupled assay, electron transfer system, overview
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q8RVZ8, Q8RVZ9
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
F4JZ46, Q8W493
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q9SLP6
FNR C-terminal domain harbors the NADP+ binding site
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
two transient charge-transfer complexes occur prior and upon hydride transfer in the reversible reaction, spectral properties and activities of wild-type and mutant enzymes, overview. Need for an adequate initial interaction between the 2'P-AMP portion of NADP+/H and FNR that provides subsequent conformational changes leading to charge-transfer complex formation
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
O05268
with K3[Fe(CN)6] as electron acceptor in the enzyme assay. Ferredoxin is a low-redox-potential iron-sulfur protein. BsFNR features two distinct binding domains for FAD and NADPH, the deduced mode of NADP+ binding to the BsFNR molecule is nonproductive in that the nicotinamide and isoalloxazine rings are over 15A A apart, binding structures, overview
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Synechocystis sp. 6803
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Cryptosporidium parvum IOWA-1
Q5CVU8
-, cyt c-coupled assay, electron transfer system, overview
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
-
r
2 reduced ferredoxin + NADP+ + H+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q96YN9, -
the enzyme plays an important role in the redox cycle of ferredoxin in the archaeon
-
-
r
2 reduced ferredoxin + NADP+ + H+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q96YN9, -
high specificity for NADPH, the activity with NADH is hardly observed without the addition of an external flavin
-
-
r
2 reduced ferredoxin + NADP+ + H+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Sulfolobus tokodaii 7
Q96YN9
the enzyme plays an important role in the redox cycle of ferredoxin in the archaeon, high specificity for NADPH, the activity with NADH is hardly observed without the addition of an external flavin
-
-
r
2 reduced ferricyanide + NADP+
2 oxidized ferricyanide + NADPH
show the reaction diagram
-
-
-
-
r
2,3-dichloro-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
Anabaena sp., Anabaena sp. PCC7119
-
single electron reduction potential -0.035 V
-
-
?
2,3-diglutathionyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
Anabaena sp., Anabaena sp. PCC7119
-
single electron reduction potential -0.15 V
-
-
?
2,5-dimethyl-1,4-benzoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.07 V
-
-
?
2,6-dichlorophenolindophenol + NAD(P)H
reduced 2,6-dichlorophenolindophenol + NAD(P)+
show the reaction diagram
-
diaphorase activity, cofactor specificity, overview
-
-
?
2,6-dichlorophenolindophenol + NAD(P)H
reduced 2,6-dichlorophenolindophenol + NAD(P)+
show the reaction diagram
-
high diaphorase activity
-
-
?
2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
-
2,6-dichlorophenolindophenol + NADH
NAD+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
P21890
-
-
-
r
2,6-dichlorophenolindophenol + NADP+
reduced 2,6-dichlorophenolindophenol + NADPH
show the reaction diagram
-
diaphorase activity
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
-
diaphorase activity
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
-
diaphorase activity
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
Q93RE3
diaphorase activity
-
-
?
2,6-dichlorophenolindophenol + NADPH
reduced 2,6-dichlorophenolindophenol + NADP+
show the reaction diagram
-
diaphorase activity, no activity with NADH
-
-
?
2,6-dichlorophenolindophenol + NADPH
?
show the reaction diagram
-
diaphorase reaction
-
-
ir
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
A0ZSY5
-
-
-
?
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
-
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
?
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
P21890
-
-
-
r
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
-
-
-
-
r
2,6-dichlorophenolindophenol + NADPH
NADP+ + reduced 2,6-dichlorophenolindophenol
show the reaction diagram
Arthrospira platensis IAM M-135
-
-
-
-
?
2,6-dichlorophenolindophenol + NADPH + H+
?
show the reaction diagram
P28861
-
-
-
?
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride + NADPH
? + NADP+
show the reaction diagram
C6KT68
-
-
-
?
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride + NADPH
?
show the reaction diagram
C6KT68
-
-
-
?
2-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.41 V
-
-
?
2-methyl-1,4-benzoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential 0.01 V
-
-
?
2-methyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.20 V
-
-
?
2-methyl-3-glutathionyl-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.16 V
-
-
?
2-methyl-3-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.46 V
-
-
?
2-methyl-5-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.16 V
-
-
?
5,8-dihydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.11 V
-
-
?
5-hydroxy-1,4-naphthoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.09 V
-
-
?
9,10-phenanthrenequinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.12 V
-
-
?
aclacinomycin A + NADP+
7-deoxyaklavinone + NADPH
show the reaction diagram
-
under anaerobic conditions
-
-
?
cytochrome c + NADPH + H+
?
show the reaction diagram
P28861
weakest substrate
-
-
?
daunomycin + NADP+
7-deoxydaunomycinone + NADPH
show the reaction diagram
-
under anaerobic conditions
-
-
?
daunorubicin + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.34 V
-
-
?
dibromothymoquinone + NADPH
? + NADP+
show the reaction diagram
-
diaphorase activity, no direct involvement of thiol or amino groups in the reaction
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
show the reaction diagram
-
diaphorase activity
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
show the reaction diagram
-
FNR has also diaphorase activity
-
-
?
dibromothymoquinone + NADPH
reduced dibromothymoquinone + NADP+
show the reaction diagram
Q8RVZ8, Q8RVZ9, -
FNR has also diaphorase activity
-
-
?
Fe(III)-citrate + NADH
reduced Fe(III)-citrate + NAD+
show the reaction diagram
-
-
-
-
?
Fe(III)-citrate + NADPH
reduced Fe(III)-citrate + NADP+
show the reaction diagram
-
-
-
-
?
Fe(III)-deferoxamine + NADPH + H+
?
show the reaction diagram
P28861
-
-
-
?
Fe(III)-diethylenetriamine-N,N,N,N,N-pentaacetic acid + NADPH + H+
Fe(II) + diethylenetriamine-N,N,N,N,N-pentaacetic acid + NADP+
show the reaction diagram
P28861
highest activity
-
-
?
Fe(III)-EDTA + NADH
reduced Fe(III)-EDTA + NAD+
show the reaction diagram
-
-
-
-
?
Fe(III)-EDTA + NADPH
reduced Fe(III)-EDTA + NADP+
show the reaction diagram
-
-
-
-
?
Fe(III)-EDTA + NADPH + H+
Fe(II) + EDTA + NADP+
show the reaction diagram
P28861
-
-
-
?
Fe(III)-ferrichrome + NADPH + H+
?
show the reaction diagram
P28861
-
-
-
?
Fe(III)-nitrilotriacetic acid + NADPH + H+
Fe(II) + nitrilotriacetic acid + NADP+
show the reaction diagram
P28861
-
-
-
?
ferric citrate + NADPH + H+
?
show the reaction diagram
P28861
-
-
-
?
ferric enterobactin + NADPH + H+
?
show the reaction diagram
P28861
lowest activity
-
-
?
ferricyanide + NAD(P)H
ferrocyanide + NAD(P)+
show the reaction diagram
-
diaphorase activity
-
-
?
ferricyanide + NAD(P)H
ferrocyanide + NAD(P)+
show the reaction diagram
-
high diaphorase activity
-
-
?
ferricyanide + NADH
ferrocyanide + NAD+
show the reaction diagram
C6KT68
-
-
-
?
ferricyanide + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron acceptor, single electron reduction potential 0.41 V
-
-
?
ferricyanide + NADPH
ferrocyanide + NADP+
show the reaction diagram
C6KT68
-
-
-
?
ferricyanide + NADPH
ferrocyanide + NADP+
show the reaction diagram
-
i.e. K3Fe(CN)6, diaphorase activity
-
-
?
ferricyanide + NADPH + H+
?
show the reaction diagram
P28861
best substrate
-
-
?
Fe[EDTA]- + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron acceptor, single electron reduction potential 0.12 V
-
-
?
flavodoxin + cytochrome c
reduced flavodoxin + NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
r
K3Fe(CN)6 + NAD(P)H
?
show the reaction diagram
C6KT68
-
-
-
?
K3Fe(CN)6 + NADPH
? + NADP+
show the reaction diagram
-
-
-
-
?
menogarol + NADP+
7-deoxynogarol + NADPH
show the reaction diagram
-
under anaerobic conditions
-
-
?
methyl viologen + NADPH
reduced methyl viologen + NADP+
show the reaction diagram
Q9L6V3, -
diaphorase activity
-
-
?
methyl viologen + NADPH
reduced methyl viologen + NADP+
show the reaction diagram
Rhodobacter capsulatus 37b4
Q9L6V3
diaphorase activity
-
-
?
NADH + FAD
NAD+ + reduced FAD
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADH
-
-
?
NADH + K3Fe(CN)6
NAD+ + reduced K3Fe(CN)6
show the reaction diagram
-
-
-
-
r
NADPH + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride
NADP+ + reduced 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride
show the reaction diagram
-
-
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
show the reaction diagram
-
diaphorase activity, acceptors can be complexed metals or aromatic molecules
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
show the reaction diagram
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
show the reaction diagram
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
show the reaction diagram
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is mostly irreversible, probably due to restrictions of formation of the caged radical pair and/or the covalent (C4alpha)-flavin hydroperoxide intermediates required for efficient oxygen reduction, acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
-
?
NADPH + acceptor
NADP+ + reduced acceptor
show the reaction diagram
Anabaena sp. PCC7119
-
diaphorase activity, acceptors can be complexed metals or aromatic molecules
-
-
?
NADPH + cytochrome c
NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
r
NADPH + FAD
NADP+ + reduced FAD
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
?
NADPH + ferricyanide
NADP+ + ferrocyanide
show the reaction diagram
-
diaphorase reaction
-
-
?
NADPH + ferricyanide
NADP+ + ferrocyanide
show the reaction diagram
-
diaphorase reaction
-
-
ir
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
show the reaction diagram
-
-
-
-
r
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
show the reaction diagram
-
-
-
-
r
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + K3Fe(CN)6
NADP+ + reduced K3Fe(CN)6
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
-
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
-
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
first enzyme in mitochondrial P-450-linked monooxygenase system catalyzing several steps in the biosynthesis of steroid hormones, bile acids or vitamin D3 in various tissues, key enzyme catalyzing the electron transport between NADPH generated by pentose phosphate pathway and ferredoxin in plastids of plant heterotrophic tissues
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
supports in vivo reduction of membrane bound adrenal mitochondrial P-450
-
-
-
nogalamycin + NADP+
7-deoxynogalarol + NADPH
show the reaction diagram
-
under anaerobic conditions
-
-
?
oxidized ferredoxin + NADH
reduced ferredoxin + NAD+
show the reaction diagram
-
very slow and inefficient reaction
-
-
?
oxidized ferredoxin + NADH + cytochrome c
reduced ferredoxin + NAD+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
ferredoxin is the preferred electron acceptor
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
Hydrogenobacter thermophilus expresses three ferredoxins: [4Fe-4S]-type Fd1 and Fd2, and [2Fe-2S]-type Fd3
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-, Hydrogenobacter thermophilus expresses three ferredoxins: [4Fe-4S]-type Fd1 and Fd2, and [2Fe-2S]-type Fd3
-
-
r
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
show the reaction diagram
A0ZSY5
-
-
-
?
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
?
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
oxidized ferredoxin + NADPH + cytochrome c
reduced ferredoxin + NADP+ + reduced cytochrome c
show the reaction diagram
Arthrospira platensis IAM M-135
-
-
-
-
?
oxidized flavodoxin + NADH + cytochrome c
reduced flavodoxin + NAD+ + reduced cytochrome c
show the reaction diagram
-
-
-
-
r
oxidized flavodoxin + NADPH
reduced flavodoxin + NADP+
show the reaction diagram
-
-, flavodoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
oxidized flavodoxin + NADPH + cytochrome c
reduced flavodoxin + NADP+ + reduced cytochrome c
show the reaction diagram
-
assay contains glucose-6-phosphate and glucose-6-phosphate dehydrogenase to recover NADPH
-
-
r
oxidized flavodoxin I + NADPH
reduced flavodoxin I + NADP+
show the reaction diagram
-
-
-
-
r
oxidized flavodoxin II + NADPH
reduced flavodoxin II + NADP+
show the reaction diagram
-
-
-
-
r
oxidized iodonitrotetrazolium violet + NADPH
reduced iodonitrotetrazolium violet + NADP+
show the reaction diagram
-
-
-
-
?
oxidized rubredoxin + NADP+
reduced rubredoxin + NADPH
show the reaction diagram
-
Clostridium pasteurianum rubredoxin
-
-
?
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
show the reaction diagram
A0ZSY5
-
-
-
?
phenyl-p-benzoquinone + NADPH + cytochrome c
? + NADP+ + reduced cytochrome c
show the reaction diagram
Arthrospira platensis, Arthrospira platensis IAM M-135
-
-
-
-
?
plastoquinone + NADPH
? + NADP+
show the reaction diagram
-
plastoquinones with different length of side chains from spinach, preference for short chain substrate, reaction proceeds via a FMN and a semiquinone intermediate, incorporation of the substrate into sodium cholate micelles is required for activity, micelles structure scheme
-
-
?
reduced ferredoxin + NAD(P)+
oxidized ferredoxin + NAD(P)H
show the reaction diagram
Chlorobaculum tepidum, Chlorobaculum tepidum CT1512
-
-
-
-
r
reduced ferredoxin + NAD+
oxidized ferredoxin + NADH
show the reaction diagram
-
the rate of NADH oxidation by FNR is lower than that with NADPH
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?, r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
C6KT68
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
P21890
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Q8EY89
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Q93RE3
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Q9L6V3, -
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Q8RVZ8, Q8RVZ9, -
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Q8W493, Q9FKW6
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
low activity
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme is involved in the electron transfer cascade from photosystem I to NADP+, formation of a ternary complex between photosystem I, ferredoxin, and enzyme
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
generation of NADPH
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
terminal step in the non-cyclic photosynthetic electron transfer chain
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
ferredoxin contains a [2Fe2S] cluster and binds to the concave surface of the FAD domain, association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
ferredoxin-dependent cytochrome c reduction, ferredoxin binding is independent of enzyme methylation status, positively charged residues K83 and K89 are required for activity
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
hydride transfer between FAD and NADP+, highly specific for NADP+ versus NAD+, mechnanism
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
hydride transfer of the N5 of the FAD isoalloxazine ring to the NADP+ nicotinamide ring, transfer of 2 electrons via the one-electron-carrier ferredoxin
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
plant-type ferredoxin contains a [2Fe2S] cluster, enzyme requires ferredoxin, substrate is a bulky protein, enzyme-substrate interactions involve residues R16, K72, K88, K116, E139, R264, K290, and K294, overview
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
plant-type ferredoxin contains a [2Fe2S] cluster, substrate is an acidic, bulky protein, enzyme-substrate interactions involve residues R16, K72, K75, R100, E139, R264, K290, and K294
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
recombinant ferredoxin I and II, and ferredoxin I mutants, the Fd I Q39R/S28E mutant lacks the Arg39-Glu28 residues being essential for efficient electron transfer between the cofactor and the enzyme
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
structure of the ferredoxin-enzyme complex, ferredoxin binds to the concave region of the FAD domain, overview, release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
structure of the ferredoxin-enzyme complex, release of oxidized ferredoxin is rate-limiting
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
substrate is a bulky protein
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
NADPH is the reducing agent of FPR in vivo
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
reaction is performed in presence of CoA
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Rhodobacter capsulatus 37b4
Q9L6V3
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
reaction is performed in presence of CoA
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Anabaena sp. PCC7119
-
-, association of ferredoxin with the enzyme is steered by electrostatic interactions
-
-
r
reduced ferredoxin I + NADP+
oxidized ferredoxin I + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
P21890
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Q8EY89
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Q9L6V3, -
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
flavodoxins I or II
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
generation of NADPH
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
reduced under conditions of iron deficit, when the [2Fe2S] cluster of ferredoxin cannot be assembled, enzyme is involved in dinitrogen fixation in heterocysts
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Q9L6V3, -
cytochrome c reduction activity
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
flavodoxin contains a FMN, enzyme-substrate interactions, overview
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
flavodoxin contains FMN
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
flavodoxin contains FMN, flavodoxins from Escherichia coli
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Rhodobacter capsulatus 37b4
Q9L6V3
-, cytochrome c reduction activity
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Anabaena sp. PCC7119
-
-
-
-
r
tetramethyl-1,4-benzoquinone + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron reduction potential -0.26 V
-
-
?
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
show the reaction diagram
-
[4Fe-4S]-ferredoxin of Pseudomonas putida is similar to ferredoxin FdI of Azotobacter vinelandii, the Pseudomonas putida chromosome contains two [2Fe-2S] ferredoxins (FdA and FdB), three [4Fe-4S] ferredoxins (4FdA, 4FdB and FdxA) and one flavodoxin (Fld)
-
-
r
methylviologen + NADP+
? + NADPH + H+
show the reaction diagram
-
single electron acceptor, single electron reduction potential -0.44 V
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
after cross-linking ferredoxin to ferredoxin NADP+-reductase the enzyme maintains most of the diaphorase activity and gains capacity to catalyze the NADPH-cytochrome c reaction without addition of free ferredoxin
-
-
-
additional information
?
-
-
enzyme has also little NADP-2,6-dichlorophenol indophenol diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also little NADP-2,6-dichlorophenol indophenol diaphorase activity
-
-
-
additional information
?
-
-
enzyme contains no FAD but shows NADP-specific diaphorase activity
-
-
-
additional information
?
-
-
truncated enzyme has no capacity to catalyze the ferredoxin-dependent reaction
-
-
-
additional information
?
-
-
enzyme has also low diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also ferredoxin dependent cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also ferredoxin dependent cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also indonitrotetrazolium-violet diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-cytochrome c reductase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-NAD transhydrogenase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-NAD transhydrogenase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-NAD transhydrogenase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
-
additional information
?
-
P00455
enzyme has also NADPH-diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also NADPH-diaphorase activity
-
-
-
additional information
?
-
-
enzyme has also irreversible NADPH-NAD+ transhydrogenase activity
-
-
-
additional information
?
-
-
involved in oxidative stress
-
-
-
additional information
?
-
-
pathway of cyclic electron transport includes both ferredoxin and ferredoxin-NADP+ reductase, but not the NADP+-binding site of the reductase
-
-
-
additional information
?
-
-
ferredoxin-NADP+ reductase not involved in cyclic electron transport
-
-
-
additional information
?
-
-
enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
-
-
-
additional information
?
-
-
enzyme is involved in cyclic electron transport and chlororespiration
-
-
-
additional information
?
-
-
enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview
-
-
-
additional information
?
-
-
enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview
-
-
-
additional information
?
-
-
enzyme is involved in the antioxidant response and facilitation of the provision of reduced flavodoxin for the reductionof nitrogenase
-
-
-
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
-
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
-
additional information
?
-
-
coenzyme binding causes structural rearrangements of the protein backbone
-
-
-
additional information
?
-
-
NADPH-dependent cytochrome c reductase assay for determination of activity with ferredoxin or flavodoxin as electron carrier
-
-
-
additional information
?
-
-
specificity for tightly bound electron acceptors, overview
-
-
-
additional information
?
-
-
structure-function analysis of isozymes and chimeric mutant thereof
-
-
-
additional information
?
-
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitro derivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible
-
-
-
additional information
?
-
-
the diaphorase reaction with NADPH and different electron acceptors, such as ferricyanide, complexed transition metals, substituted phenols, nitroderivatives, tetrazolium salts, NAD+, viologens, quinones, and cytochromes, is highly irreversible
-
-
-
additional information
?
-
-
the enzyme also shows NAD(P)H oxidase activity, overview
-
-
-
additional information
?
-
-
the enzyme binds to phycocyanin hexamers
-
-
-
additional information
?
-
-
the enzyme is asscoiated to phycobilin pigments
-
-
-
additional information
?
-
-
Fpr also catalyzes irreversible electron transfer (diaphorase activity), which drives the oxidation of NADPH in a wide variety of electron acceptors, such as viologens, quinines, complexed transition metals, and tetrazolium salts
-
-
-
additional information
?
-
-
FPR supports the efficient degradation of heme by heme oxygenase
-
-
-
additional information
?
-
-
shows negligible activity when NADP+ is replaced with NAD+
-
-
-
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
-
additional information
?
-
Q8RVZ8, Q8RVZ9
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
-
additional information
?
-
F4JZ46, Q8W493
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
-
additional information
?
-
Q9SLP6
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
-
additional information
?
-
-
in vitro, the enzyme catalyses the NADPH-dependent reduction of various substrates, including ferredoxin, the analogue of its redox centre-ferricyanide, and the analogue of quinones, which is dibromothymoquinone
-
-
-
additional information
?
-
-
the enzyme also shows NADPH-dependent cyt c reductase activity
-
-
-
additional information
?
-
Anabaena sp. PCC7119
-
phylogenetic evolution, relationships, and classification, overview
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q8RVZ8, Q8RVZ9
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q8RVZ8, Q8RVZ9
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
F4JZ46, Q8W493
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
-, Q5CVU8
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
O05268
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q9SLP6
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Synechocystis sp. 6803
-
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Cryptosporidium parvum IOWA-1
Q5CVU8
-
-
-
r
2 reduced ferredoxin + NADP+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Triticum aestivum Paragon
Q8RVZ8, Q8RVZ9
-
-
-
r
2 reduced ferredoxin + NADP+ + H+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Q96YN9, -
the enzyme plays an important role in the redox cycle of ferredoxin in the archaeon
-
-
r
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
first enzyme in mitochondrial P-450-linked monooxygenase system catalyzing several steps in the biosynthesis of steroid hormones, bile acids or vitamin D3 in various tissues, key enzyme catalyzing the electron transport between NADPH generated by pentose phosphate pathway and ferredoxin in plastids of plant heterotrophic tissues
-
-
?
NADPH + oxidized ferredoxin
NADP+ + reduced ferredoxin
show the reaction diagram
-
supports in vivo reduction of membrane bound adrenal mitochondrial P-450
-
-
-
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
-
-
-
r
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
ferredoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
oxidized ferredoxin + NADPH
reduced ferredoxin + NADP+
show the reaction diagram
-
Hydrogenobacter thermophilus expresses three ferredoxins: [4Fe-4S]-type Fd1 and Fd2, and [2Fe-2S]-type Fd3
-
-
r
oxidized flavodoxin + NADPH
reduced flavodoxin + NADP+
show the reaction diagram
-
flavodoxin-dependent enzyme radical generation and enzyme activation, electron supply from NADPH
-
-
?
oxidized flavodoxin I + NADPH
reduced flavodoxin I + NADP+
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
-
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Q9L6V3, -
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
delivers NADPH or reduced ferredoxin for several metabolic reactions, involved in photosynthesis, enzyme-substrate interactions, overview
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme catalyzes the final step of photosynthetic electron transfer from the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation in plants, in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme catalyzes the final step of photosynthetic electron transfer fron the iron-sulfur protein ferredoxin reduced by photosystem I to NADP+ providing NADPH necessary for CO2 assimilation, enzyme is involved in dinitrogen fixation in heterocysts
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme is involved in protection against oxidative stress, and in activation of anaerobic enzymes
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
enzyme is involved in the electron transfer cascade from photosystem I to NADP+, formation of a ternary complex between photosystem I, ferredoxin, and enzyme
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
generation of NADPH
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
in root and heterotrophic tissue, the reaction is driven towards ferredoxin reduction, reaction is part of nitrogen assimilation in nonphotosynthetic tissues
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
responsible for NADPH generation
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
reverse reaction is involved in activation of enzymes that participate in anaerobic metabolism, removal of free radicals gegnerated during the metabolsim
-
-
r
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
-
terminal step in the non-cyclic photosynthetic electron transfer chain
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Rhodobacter capsulatus 37b4
Q9L6V3
-
-
-
?
reduced ferredoxin + NADP+
oxidized ferredoxin + NADPH
show the reaction diagram
Anabaena sp. PCC7119
-
-
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Q9L6V3, -
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
flavodoxins I or II
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
generation of NADPH
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
-
reduced under conditions of iron deficit, when the [2Fe2S] cluster of ferredoxin cannot be assembled, enzyme is involved in dinitrogen fixation in heterocysts
-
-
r
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Rhodobacter capsulatus 37b4
Q9L6V3
-
-
-
?
reduced flavodoxin + NADP+
oxidized flavodoxin + NADPH
show the reaction diagram
Anabaena sp. PCC7119
-
-
-
-
r
[4Fe-4S]-ferredoxin + NADPH
reduced [4Fe-4S]-ferredoxin + NADP+
show the reaction diagram
-
[4Fe-4S]-ferredoxin of Pseudomonas putida is similar to ferredoxin FdI of Azotobacter vinelandii, the Pseudomonas putida chromosome contains two [2Fe-2S] ferredoxins (FdA and FdB), three [4Fe-4S] ferredoxins (4FdA, 4FdB and FdxA) and one flavodoxin (Fld)
-
-
r
2 reduced ferredoxin + NADP+ + H+
2 oxidized ferredoxin + NADPH
show the reaction diagram
Sulfolobus tokodaii 7
Q96YN9
the enzyme plays an important role in the redox cycle of ferredoxin in the archaeon
-
-
r
additional information
?
-
-
involved in oxidative stress
-
-
-
additional information
?
-
-
pathway of cyclic electron transport includes both ferredoxin and ferredoxin-NADP+ reductase, but not the NADP+-binding site of the reductase
-
-
-
additional information
?
-
-
ferredoxin-NADP+ reductase not involved in cyclic electron transport
-
-
-
additional information
?
-
-
enzyme is involved in anaerobic metabolism, phylogenetic evolution, relationships, and classification, overview
-
-
-
additional information
?
-
-
enzyme is involved in cyclic electron transport and chlororespiration
-
-
-
additional information
?
-
-
enzyme is involved in nitrogenase reduction, phylogenetic evolution, relationships, and classification, overview
-
-
-
additional information
?
-
-
enzyme is involved in photosynthesis and nitrite assimilation, phylogenetic evolution, relatiionships, and classification, overview
-
-
-
additional information
?
-
-
enzyme is involved in the antioxidant response and facilitation of the provision of reduced flavodoxin for the reductionof nitrogenase
-
-
-
additional information
?
-
-
phylogenetic evolution, relatiionships, and classification, overview
-
-
-
additional information
?
-
-
phylogenetic evolution, relationships, and classification, overview
-
-
-
additional information
?
-
-
FNR interacts with several partners, e.g. the NDH complex in the thylakoids, association of FNR with cytochrome b6f or PGRL1 or the photosystem I, overview
-
-
-
additional information
?
-
Q8RVZ8, Q8RVZ9
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
-
additional information
?
-
F4JZ46, Q8W493
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
-
additional information
?
-
Q9SLP6
FNR is bound to the oxygen evolving complex proteins, and also to a heat stable socalled connectein protein of 10 kDa, which binds two molecules of FNR and is involved in membrane binding. Chloroplast FNR co-purifies with the Cyt b6f complex, while unlike bacterial FNR, it does not bind to NDH complexes
-
-
-
additional information
?
-
Anabaena sp. PCC7119
-
phylogenetic evolution, relationships, and classification, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2Fe-2S-center
-
-
-
FAD
-
1 mol FAD per mol of enzyme; flavoprotein
FAD
-
flavoprotein
FAD
-
flavoprotein
FAD
-
flavoprotein
FAD
-
in contrast to stromal reductase, the solubilized and purified membrane-bound enzyme contains no FAD
FAD
-
1 mol FAD per mol of enzyme; flavoprotein
FAD
-
involved in electron transfer in the reaction
FAD
-
binding and hydride/electron transfer mechanism
FAD
-
extended conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
-
folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
-
folded conformation, modeling of conformation of C4alpha polypeptide backbone and FAD, binding domain is N-terminal
FAD
-
extended conformation, interaction via Tyr96, direct electron transfer between FAD and ferredoxin [2Fe2S] center, modeling of conformation of C4alpha polypeptide backbone and FAD
FAD
-
0.98 mol FAD tightly bound to 1 mol of enzyme
FAD
-
flavoenzyme
FAD
-
noncovalently bound prosthetic group; noncovalently bound prosthetic group, binding domain structure, ferredoxin binds to the concave region of the FAD domain
FAD
-
noncovalently bound
FAD
Q9L6V3
prosthetic group, tightly bound, can be released by heat denaturation
FAD
-
prosthetic group, flavoenzyme
FAD
-
involved in reaction splitting a two-electron-reaction into 2 one-electron-reactions
FAD
-
binding domain structure, structure-function relationship
FAD
-
48% FAD semiquinone at the equilibrium, pH 7.0
FAD
-
structure contains two domains harboring FAD and NAD(P)H binding sites
FAD
-
FAD is reduced rapidly and completely when the enzyme reacts with NADPH, while in contrast, addition of NADH results in very slow and inefficient reduction
FAD
-
free FAD serves as an electron carrier
FAD
-
noncovalently bound
FAD
-
dependent on
FAD
F4JZ46, Q8W493
FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding; FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding
FAD
Q8RVZ8, Q8RVZ9
FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding; FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding
FAD
Q9SLP6
FNR harbors one molecule of noncovalently bound FAD as a prosthetic group, it functions as an one-to-two electron switch by reduction of FAD to a semiquinone form FADH, followed by another round of reduction to FADH-, and hydride transfer from FADH- to NADP+. The FNR N-terminal domain is involved in FAD binding
FAD
-
noncovalently bound, the flavin can adopt three different redox forms as the oxidized quinone form FAD, the one-electron reduced semiquinone radical form FADHradical, and the fully reduced quinol form FADH2
FAD
O05268
BsFNR features two distinct binding domains for FAD and NADPH, binding structure, overview. A unique C-terminal extension covers the re-face of the isoalloxazine moiety of FAD. Tyr50 in the FAD-binding region and His324 in the Cterminal extension stack on the si- and re-faces of the isoalloxazine ring of FAD, respectively
FAD
-
one molecule of noncovalently bound
FAD
P28861
contains FAD, the Km for FAD is 0.0429 mM
FAD
Q96YN9, -
contains 0.46 mol FAD/mol subunit
Ferredoxin
-
activation of diaphorase and transhydrogenase
-
Ferredoxin
-
[2Fe2S] cluster containing, ferredoxin I and II, and ferredoxin I mutants, the latter lacking the Arg39-Glu28 residues being essential for efficient electron transfer between the cofactor and the enzyme, the Fd I Q39R/S28E mutant is unstable and rapidly loose the [2Fe2S] cluster, the mutant shows 5.5fold reduced electron transfer rates compared to Fd I, ferredoxin II mutant D64N is about half as efficient as cofactor as the wild-type ferredoxin I and II are
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
Ferredoxin
-
-
-
Ferredoxin
Q8RVZ8, Q8RVZ9
;
-
flavin
-
flavoprotein
FMN
-
protein contains flavin mononucleotide instead of FAD
FMN
-
free FMN serves as an electron carrier
NAD(P)H
-
NADPH is absolutely preferred over NADH by the wild-type isozymes
NAD+
-
enzyme reduces NADP+ and NAD+, specific for NADP+ reduction under physiological conditions
NAD+
-
diaphorase activity, low activity with
NADH
-
diaphorase activity, low activity with
NADH
-
diaphorase activity
NADH
-
structure contains two domains harboring FAD and NAD(P)H binding sites
NADP+
-
requirement for NADPH
NADP+
-
enzyme reduces NADP+ and NAD+, specific for NADP+ reduction under physiological conditions
NADP+
-
reductase is covalently cross linked to Azotobacter vinelandii flavodoxin
NADP+
-
requirement for NADPH
NADP+
-
binding and hydride transfer mechanism
NADP+
-
C-terminal binding domain
NADP+
-
C-terminal binding domain
NADP+
-
interaction via Tyr314, binding site at the C-terminus
NADP+
-
binding domain structure, binding mechanism
NADP+
-
binding domain structure of the plant-type enzyme, binding mechanism
NADP+
-
binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview
NADP+
-
binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADP+
-
binding mechanism
NADP+
-
binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADP+
-
binding domain structure, binding mechanism
NADP+
-
binding structure, binding causes conformational changes in the enzyme and creation of a new binding pocket near the FAD binding site
NADP+
-
interaction with the enzyme, complex structure, specificity-determining structures, overview
NADP+
-
interaction with the enzyme, complex structure, specificity-determining structures, overview
NADP+
-
binding domain structure, structure-function relationship
NADP+
Q8RVZ8, Q8RVZ9
;
NADP+
Q8W493, Q9FKW6
;
NADPH
-
reverse reaction: preferred cofactor, poor activity with NADH
NADPH
-
binding and hydride transfer mechanism
NADPH
-
C-terminal binding domain
NADPH
-
C-terminal binding domain
NADPH
-
interaction via Tyr314, binding site at the C-terminus
NADPH
-
binding domain structure, binding mechanism
NADPH
-
binding domain structure of the plant-type enzyme, binding mechanism
NADPH
-
binding mechanism, cofactor is tightly bound, binding site structure and involved residues, overview
NADPH
-
binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADPH
-
binding mechanism
NADPH
-
binding domain structure, binding mechanism, binding site structure and involved residues, overview
NADPH
-
binding domain structure, binding mechanism
NADPH
-
diaphorase activity
NADPH
-
binding domain structure, structure-function relationship
NADPH
-
structure contains two domains harboring FAD and NAD(P)H binding sites
FMN
Q96YN9, -
activates. Vmax is 1.38 and 21.8 U/mg (at 70C) in the absence and presence of 1 mM FMN
additional information
-
-
-
additional information
-
no activity with NADH
-
additional information
-
poor activity with NAD(H)
-
additional information
-
the coenzyme specificity determining structures are located in the 2'-phosphate NADP+ and pyrophosphate binding region of amino acid residues 155-160, 261-268, and S233, R224, R233, and Y235, coenzyme binding causes structural rearrangements of the protein backbone, binding and interaction mechanism with the enzyme, overview
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Fe2+
-
in the iron-sulfur center of ferredoxin
Iron
-
enzyme contains an [2Fe2S] cluster as prosthetic group involved in the reaction
Iron
-
[2Fe-2S] cluster
NaCl
-
stimulation at 0.1 M
NH4+
-
activator of ferredoxin-NADP+ reductase
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2',5'-ADP
-
competitive inhibition
2',5'-ADP
-
competitive inhibition, but there could also be a non-competitive component caused by binding at a weak secondary NADP+ binding site
2',5'-ATP-ribose
-
competitive inhibition, competitive in forming complexes with reductase
2'-AMP
-
when 2,6-dichlorophenolindophenol serves as electron acceptor
adenosine 2',5'-diphosphate
-
-
Butanedione
-
inhibitor of transhydrogenase and diaphorase activity, reacts with arginine residue involved in binding of pyridine nucleotides
Cd2+
-
70% inhibition, uncompetitive to dibromothymoquinone, noncompetitive inhibition of NADPH oxidation, Zn2+ diminishes the inhibitory effect for dibromothymoquinone reduction, but enhances inhibition of ferricyanide reduction, inhibitory effect on ferricyanide reduction, but on dibromothymoquinone reduction, is abolished by addition of 2-mercaptoethanol or histidine, inhibition mechnanism, overview
Cd2+
-
noncompetitive type of inhibition, effect of cadmium binding is significant disturbance in the electron transfer process from FAD to dibromothymoqinone, but less interference with the reduction of ferricyanide. It causes a strong inhibition of ferredoxin reduction, indicating that Cd-induced changes in the FNR structure disrupt ferredoxin binding. Iodoacetamide blocks the sensitivity to Cd2+ inhibition. pH-Dependent inhibition: to interact with cadmium in a mode which leads to inhibition, the cysteine residues of FNR have to be charged. Almost no inhibition in pH lower than pH 7.7, while in pH higher than pH 8.1 the reduction of activity caused by cadmium ions increases, FNR cysteine-peptide mapping, overview. Triticum aestivum FNR is more sensitive to lower cadmium concentrations than the Spinacia oleracea enzyme
diphosphate
-
inhibitor of ferredoxin-dependent photoreduction
disulfodisalicylidenepropane-1,1-diamine
-
inhibits all reactions except photoreduction of cytochrome c
Ferredoxin
-
oxidized ferredoxin inhibits both the first and second one-electron reduction
-
Ferredoxin
-
competitive inhibitor with NADPH in dichlorophenolindophenol reductase reaction
-
Ferredoxin
-
inhibition of electron transfer at higher electron acceptor rate
-
flavodoxinI/II
-
inhibition of electron transfer at higher electron acceptor rate
-
guanidine hydrochloride
-
0.1 M guanidine hydrochloride reduces activity by 30%, 0.2 M guanidine hydrochloride by 60%, and 0.4 M guanidine hydrochloride by 85%, concentrations over 0.7 M guanidine hydrochloride eliminate activity
heparin
-
binds to the enzyme, inhibits ferredoxin and NADPH binding to the enzyme
Mercurials
-
-
-
Mg2+
-
inhibits reduction of plastoquinone incorporated into sodium cholate micelles
myristyltrimethylammonium bromide
-
inhibits reduction of plastoquinone almost completely at 15 mM
N-ethyl-3(3-dimethylaminopropyl)carbodiimide inactivates ferredoxin-NADP+ reductase
-
-
-
N-ethylmaleimide
-
-
N6-(6-aminohexyl)-2',5'-ADP
-
competitive inhibition
NaCl
-
high concentration
NaCl
-
ferredoxin-dependent activity decreases with increasing NaCl concentration and disappears at concentrations over 0.5 M NaCl
NaCl
A0ZSY5
ferredoxin-dependent activity decreases with increasing NaCl concentration and disappears at concentrations over 0.5 M NaCl
NADPH
-
reversible inhibition, is turned to irreversible in presence of 4 M urea
octylglucoside
-
inhibits reduction of plastoquinone
oxidized ferredoxin
-
inhibits binding of reduced ferredoxin and reduction of flavin
SDS
-
inhibits reduction of plastoquinone almost completely at 15 mM
Triazine dyes
-
interaction with the enzyme, competitive inhibitor of NADPH in ferricyanide reduction assays
-
Triazine dyes
-
competitive inhibition of diaphorase activity
-
Triton X-100
-
inhibits reduction of plastoquinone
Urea
-
1 M urea reduces activity by 20%, 2 M urea by 40%, and 3 M urea by 80%, concentrations over 5 M urea eliminate activity
Zn2+
-
80% inhibition
[Cr[CN]6]4-
-
binds to the enzyme
-
MgCl2
-
inhibits at lower salt concentrations
additional information
-
inhibited by specific antibodies
-
additional information
-
enzyme is activated by light and inactivated by dark
-
additional information
-
association of ferredoxin inhibits binding of NADPH
-
additional information
-
activity decreases with elevated ionic strength
-
additional information
-
histidine and 2-mercaptoethanol are not inhibitory
-
additional information
-
gradual decrease in activity according to biphasic kinetics within 120 min, 80% of maximal activity can be restored by addition of DTNB or fluoresamine, dibromothymoquinone influences the inhibitory pattern and modifies the enzyme conformation
-
additional information
-
induction of FprB expression is not affected by oxidative stress agents, such as paraquat, menadione, H2O2, and t-butyl hydroperoxide
-
additional information
-
FNR is inactivated after prolonged dark exposure
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Fe2+
-
Fprs are induced by Fe2+ depletion but not by Fe2+ excess
-
Fe3+
-
0.5 microM Fe(III)-citrate and 0.5 microM Fe(III)-EDTA induces Fprs
-
Ferredoxin
-
enhances diaphorase reaction with NADPH, but not with NADH
-
Ferredoxin
-
highly stimulates NADPH oxidation
-
Flavodoxin
-
stimulates about 2fold the reduction of NADP+
-
H2O2
-
1.0 mM, oxidative stress induces Pseudomonas putida FprA but not FprB
NaCl
-
0.51 M and 0.85 M NaCl increases Fpr expression
NaCl
-
quinone-dependent activity decreases at concentration below 0.1 M and over 0.5 M
NaCl
A0ZSY5
quinone-dependent activity decreases at concentrations below 0.1 M and over 0.7 M
NADP+
-
stimulates binding of reduced ferredoxin and reduction of flavin
paraquat
-
0.5 mM, oxidative stress induces Pseudomonas putida FprA but not FprB
polylysine
-
activator of ferredoxin-NADP+ reductase
Sodium cholate
-
stimulated NADPH oxidation, especially in presence of plastoquinone substrate
tert-butyl hydroperoxide
-
0.5 mM, oxidative stress induces Pseudomonas putida FprA but not FprB
Tic62
-
required for FNR binding to thylakoid membranes, FNR-binding motifs, overview
-
TROL
-
required for FNR binding to thylakoid membranes, FNR-binding motifs, overview
-
menadione
-
1.0 mM, oxidative stress induces Pseudomonas putida FprA but not FprB
additional information
-
acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
additional information
-
acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
additional information
-
acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
additional information
-
acceptors enhance the oxidation reaction severalfold, e.g. ferredoxin, flavodoxin, viologens, nitroderivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide; acceptors enhance the oxidation reaction several fold, e.g. ferredoxin, flavodoxin, viologens, nitro derivatives, and quinones, that can readily engage in oxygen-dependent redox cycling leading to formation of superoxide
-
additional information
-
low CO2 enhances the expression and activity of FNR and the cyclic photosystem I mediated by FNR
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.036
-
2,6-dichlorophenol indophenol
-
diaphorase activity enzyme I
0.047
-
2,6-dichlorophenol indophenol
-
diaphorase activity enzyme II
0.01
0.016
2,6-dichlorophenol-indophenol
-
NADPH-2,6-dichlorophenol-indophenol diaphorase activity
0.056
-
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25C, with NADH
0.058
-
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25C, with NADPH
0.095
-
2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride
-
at 25C in 200 mM Tris-HCl (pH 9.0), containing 70 mM NaCl and 0.1% Triton-X100
0.0119
-
dibromothymoquinone
-
-
0.0132
-
dibromothymoquinone
-
in presence of Cd2+
0.015
-
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25C, with NADH
0.022
-
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25C, with NADPH
0.00364
-
Fe(III)-EDTA
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25C
0.0396
-
Fe(III)-EDTA
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25C
0.00027
-
Ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 28 mM
-
0.0005
-
Ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 100 mM
-
0.0008
-
Ferredoxin
-
Plasmodium falciparum ferredoxin PfFd is tested;using cytochrome c as electron acceptor
-
0.0009
-
Ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 200 mM
-
0.0012
-
Ferredoxin
-
-
-
0.0025
-
Ferredoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 100 mM
-
0.0026
-
Ferredoxin
-
native enzyme, pH 8.0, 30C
-
0.0028
-
Ferredoxin
-
mutant lacking amino acids 81 to 118, pH 8.2, 25C
-
0.0035
-
Ferredoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 200 mM
-
0.0038
-
Ferredoxin
-
enzyme II
-
0.0043
-
Ferredoxin
-
enzyme I
-
0.0043
-
Ferredoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 28 mM
-
0.0045
0.0046
Ferredoxin
-
ferredoxin-dependent cytochrome c reductase activity
-
0.005
-
Ferredoxin
-
-
-
0.0058
-
Ferredoxin
-
pH 8.0, 13C, mutant Y308F
-
0.0065
-
Ferredoxin
-
pH 8.0, 13C, wild-type enzyme
-
0.0066
-
Ferredoxin
-
recombinant enzyme, pH 8.0, 30C
-
0.009
-
Ferredoxin
-
pH 8.0, 13C, mutant Y308S
-
0.011
-
Ferredoxin
-
pH 8.0, 13C, wild-type enzyme
-
0.012
-
Ferredoxin
-
pH 8.0, 25C
-
0.017
-
Ferredoxin
-
pH 8.0, 13C, mutant Y308W
-
0.018
-
Ferredoxin
-
wild-type, pH 8.2, 25C
-
0.02
-
Ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 100 mM
-
0.021
-
Ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 200 mM
-
0.023
-
Ferredoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 100 mM; recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 28 mM
-
0.049
-
Ferredoxin
-
35 kDa enzyme
-
0.051
-
Ferredoxin
-
pH 8.0, 13C, mutant Y303F
-
0.053
-
Ferredoxin
-
32 kDa enzyme
-
0.1
-
Ferredoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 28 mM
-
0.4
-
Ferredoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 200 mM
-
0.0025
-
ferredoxin I
-
pH 7.0, 15C, wild-type root isozyme
-
0.0026
-
ferredoxin I
-
pH 7.0, 15C, wild-type leaf isozyme
-
0.0027
-
ferredoxin I
-
pH 7.0, 15C, recombinant chimeric enzyme
-
0.0114
-
ferredoxin I
-
wild-type cofactor, pH 7.5, 25C
-
0.0017
-
ferredoxin II
-
wild-type cofactor, pH 7.5, 25C
-
0.0053
-
ferredoxin II mutant D64N
-
pH 7.5, 25C
-
0.0115
-
ferredoxin II mutant Q39R/S28E
-
pH 7.5, 25C
-
0.0006
-
Flavodoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 200 mM
-
0.0009
-
Flavodoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 100 mM
-
0.0024
-
Flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 28 mM
-
0.008
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59A
-
0.0082
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I92A
-
0.0089
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59E
-
0.0096
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I92E
-
0.01
-
Flavodoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 28 mM
-
0.0109
-
Flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 100 mM
-
0.0167
-
Flavodoxin
-
pH 8.0, 13C, wild-type enzyme
-
0.02
-
Flavodoxin
-
pH 8.0, 13C, mutant Y308F
-
0.0266
-
Flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 200 mM
-
0.033
-
Flavodoxin
-
pH 8.0, 13C, wild-type enzyme
-
0.033
-
Flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 28 mM
-
0.033
-
Flavodoxin
-
using cytochrome c as electron acceptor
-
0.0338
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59A/I92A
-
0.04
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59E/I92E
-
0.043
-
Flavodoxin
-
pH 8.0, 13C, mutant Y303F
-
0.06
-
Flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 100 mM
-
0.0701
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57E
-
0.0767
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57R
-
0.0891
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57K
-
0.099
-
Flavodoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 28 mM
-
0.127
-
Flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 200 mM
-
0.0076
-
flavodoxin I
-
pH 8.0, 25C
-
0.004
-
flavodoxin II
-
pH 8.0, 25C
-
0.03
0.0547
iodonitrotetrazolium violet
-
4 different fractions after ferredoxin-Sepharose chromatography
0.00112
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.00235
-
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00273
-
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00298
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.00338
-
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.00464
-
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.00616
-
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0065
-
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.007
-
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.00717
-
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.00802
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.00822
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00866
-
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.00933
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.00943
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.01063
-
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.01163
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.01238
-
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.0129
-
NADH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.01866
-
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.02363
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.0394
-
NADH
P21890
mutant T155G/A160T/L263P/Y303S, called PP3CT
0.05625
-
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.0632
-
NADH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.064
-
NADH
P21890
mutant T155G/A160T/L263P/R264P/G265P, called PP5
0.068
-
NADH
-
recombinant enzyme, pH 8.2, 25C, with Fe(CN)63-
0.083
-
NADH
-
recombinant enzyme, pH 8.2, 25C, with 2,6-dichlorophenolindophenol
0.1076
-
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.18
-
NADH
-
mutant T155G, pH 8.0
0.39
-
NADH
-
mutant T155G/A160T/L263P, pH 8.0
0.39
-
NADH
P21890
mutant T155G/A160T/L263P, called PP3
0.51
-
NADH
-
mutant T155G/A160T, pH 8.0
0.63
-
NADH
-
mutant L263A, pH 8.0
0.65
-
NADH
-
mutant L263P, pH 8.0
0.72
-
NADH
-
25C, pH 8.2; with K3Fe(CN)6 as cosubstrate, at 25C, in 100 mM Tris-HCl (pH 8.2)
0.8
-
NADH
-
wild-type enzyme, pH 8.0
0.8
-
NADH
P21890
wild type enzyme of Anabaena sp.
1.25
-
NADH
P21890
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
1.323
-
NADH
P21890
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
1.5
-
NADH
-
mutant S223D/R233L/Y235F, pH 8.0
2.3
-
NADH
-
mutant R233L/Y235F, pH 8.0
3
-
NADH
-
mutant T155G/R224Q/R233L/Y235F, pH 8.0
4.2
-
NADH
-
pH 7.0, 15C, recombinant chimeric enzyme
4.3
-
NADH
-
mutant R224Q/R233L/Y235F, pH 8.0
12
-
NADH
-
mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
0.00722
-
NADP+
-
-
0.00045
-
NADPH
-
recombinant enzyme, pH 8.2, 25C, with Fe(CN)63-
0.00083
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00089
-
NADPH
-
recombinant enzyme, pH 8.2, 25C, with 2,6-dichlorophenolindophenol
0.00094
-
NADPH
-
-
0.0011
-
NADPH
-
in a quinone-dependent cytochrome c reduction assay
0.0011
-
NADPH
A0ZSY5
in a quinone-dependent cytochrome c reduction assay
0.00111
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.0012
-
NADPH
-
wild-type, 30C, pH 8.0
0.0018
-
NADPH
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in 50 mM sodium phosphate (pH 7.0), at 25C
0.00181
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
0.00191
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor; for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
0.0024
-
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30C, pH 8.0
0.00245
-
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0026
-
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30C, pH 8.0
0.00263
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
0.0031
-
NADPH
-
in presence of Cd2+
0.00326
-
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
0.0034
-
NADPH
-
recombinant mutant E139Q, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
0.0037
-
NADPH
-, Q5CVU8
pH 7.4, temperature not specified in the publication, recombinant enzyme
0.00397
-
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.004
-
NADPH
-
in a ferredoxin-dependent cytochrome c reduction assay
0.004
-
NADPH
A0ZSY5
in a ferredoxin-dependent cytochrome c reduction assay
0.0041
-
NADPH
P21890
mutant T155G/A160T/L263P/Y303S, called PP3CT
0.00457
-
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.00459
-
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.0047
-
NADPH
-
recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
0.00479
-
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
0.005
-
NADPH
-
-
0.0055
-
NADPH
-
using cytochrome c as electron acceptor
0.0058
-
NADPH
-
recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
0.0058
-
NADPH
-
-
0.00587
-
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
0.006
-
NADPH
-
recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
0.006
-
NADPH
-
wild-type enzyme, pH 8.0
0.006
-
NADPH
P21890
wild type enzyme of Anabaena sp.
0.00615
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.00625
-
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.00636
-
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.00666
-
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.00686
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
0.007
-
NADPH
-
native enzyme, pH 8.0, 30C
0.0074
-
NADPH
-
pH 7.0, 15C, recombinant chimeric enzyme, diaphorase activity
0.00751
-
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.0092
-
NADPH
-
-
0.0094
-
NADPH
-, Q5CVU8
pH 8.2, temperature not specified in the publication, recombinant enzyme
0.01
-
NADPH
-
INT as electron acceptor
0.01
-
NADPH
-
using K3Fe(CN)6 as electron acceptor
0.011
0.035
NADPH
-
ferredoxin-dependent cytochrome c reductase activity
0.011
-
NADPH
-
in a 2,6-dichlorophenolindophenol reduction assay
0.01177
-
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
0.012
-
NADPH
-
K3Fe(CN)6 as electron acceptor
0.012
-
NADPH
-
pH 7.0, 15C, wild-type root isozyme, diaphorase activity
0.012
-
NADPH
-
mutant T155G/A160T/L263P, pH 8.0
0.012
-
NADPH
P21890
mutant T155G/A160T/L263P, called PP3
0.01319
-
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
0.01424
-
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
0.015
-
NADPH
-
mutant L263A, pH 8.0
0.015
-
NADPH
-
wild-type, pH 9.0, 25C
0.01544
-
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
0.016
-
NADPH
-
mutant lacking amino acids 81 to 118, pH 9.0, 25C
0.019
-
NADPH
-
mutant L263P, pH 8.0
0.0195
-
NADPH
-, Q8EY89
in 50 mM Tris-HCl, pH 8, at 30C
0.02
-
NADPH
A0ZSY5
in a 2,6-dichlorophenolindophenol reduction assay
0.022
-
NADPH
-
mutant T155G/A160T, pH 8.0
0.022
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
0.023
-
NADPH
-
mutant T155G, pH 8.0
0.023
-
NADPH
P21890
mutant T155G/A160T/L263P/R264P/G265P, called PP5
0.0242
-
NADPH
-, Q5CVU8
pH 6.8, temperature not specified in the publication, recombinant enzyme
0.028
-
NADPH
-
-
0.02967
-
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
0.03
-
NADPH
-
-
0.033
0.062
NADPH
-
NADPH-2,6-dichlorophenol indophenol diaphorase activity
0.033
-
NADPH
-
recombinant enzyme, pH 8.0, 30C
0.035
-
NADPH
-
pH 7.0, 15C, wild-type leaf isozyme, diaphorase activity
0.035
-
NADPH
-
both wild-type and mutant Q242R
0.036
0.043
NADPH
-
multiple forms of ferredoxin-NADP+ reductase
0.036
-
NADPH
-
25C, pH 8.2; with K3Fe(CN)6 as cosubstrate, at 25C, in 100 mM Tris-HCl (pH 8.2)
0.036
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor
0.05
-
NADPH
-
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
0.057
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
0.059
-
NADPH
-
diaphorase activity enzyme I
0.067
-
NADPH
-
diaphorase activity enzyme II
0.071
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
0.14
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
0.35
-
NADPH
-
cosubstrate 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride, 25C, pH 9.0; with 2-(p-iodophenyl)-3-(p-nitrophenyl)-5-phenyltetrazolium chloride as cosubstrate, at 25C, in 100 mM Tris-HCl (pH 8.2)
0.37
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
0.4
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
0.52
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
0.57
-
NADPH
-
2,6-dichlorophenolindophenol reduction, pH 7.0, 24C
0.8
-
NADPH
Q9L6V3
diaphorase activity, pH 8.0
1.366
-
NADPH
P21890
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
1.7
-
NADPH
-
mutant R233L/Y235F, pH 8.0
1.8
-
NADPH
-
above, mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
2.7
-
NADPH
-
mutant T155G/R224Q/R233L/Y235F, pH 8.0
3.6
-
NADPH
-
mutant R224Q/R233L/Y235F, pH 8.0
0.54
-
oxidized ferredoxin
-
with NADPH, pH 7.0, 24C
0.009
-
reduced flavodoxin
Q9L6V3
pH 8.0
0.097
0.1
K3Fe(CN)6
-
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
increasing light intensity reduces Km; increasing NH4Cl concentration enhances Km; Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
enzyme covalently cross-linked to flavodoxin; Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH; Km value of different mutants
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
enzyme reacts slower with different mutants of ferredoxin than with wild type ferredoxin; Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
Km value increases with pH
-
additional information
-
additional information
-
thermodynamics and kinetics, measurement of direct electron transfer by stopped-flow spectrophotometry
-
additional information
-
additional information
-
below 0.1 mM, oxidized ferredoxin with NADH, pH 7.0, 24C
-
additional information
-
additional information
-
stopped-flow and laser flash kinetic measurements, steady-state kinetics, dissociation constants and reduction potentials of wild-type and mutant enzymes
-
additional information
-
additional information
-
steady-state kinetics and dissociation constants of NADPH-enzyme complex, wild-type isozymes and recombinant chimera
-
additional information
-
additional information
-
forward and reverse reactions follow different kinetic mechanism, overview
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
stopped-flow kinetics measurements, pH 8.0, 13C, steady-state kinetics for wild-type and mutant enzymes dependent on ionic strength, overview
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics, rapid thermal inactivation of reduced enzyme and drop of activity
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetics, wild-type and mutant enzymes
-
additional information
-
additional information
-
detailed binding kinetics, detailed reaction kinetics, enzyme-substrate complex formation
-
additional information
-
additional information
-
gradual decrease in activity according to biphasic kinetics within 120 min
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
analysis of kinetic rate constants for the reaction of enzyme with NADP+/NADPH
-
additional information
-
additional information
-
Fpr showed high specificity for NADPH; Km value for NADPH is <5 microMol, whereas that for NADH is above 2 mM
-
additional information
-
additional information
-
stopped flow kinetic analysis
-
additional information
-
additional information
-
Stopped-flow pre-steady-state kinetics, overview
-
additional information
-
additional information
-, Q5CVU8
Michaelis-Menten kinetics, overview
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
21
-
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25C, with NADH
25.6
-
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.2, 25C, with NADPH
35
-
2,6-dichlorophenolindophenol
-
native enzyme, pH 8.0, 30C
37
-
2,6-dichlorophenolindophenol
-
recombinant enzyme, pH 8.0, 30C
12.6
-
dibromothymoquinone
-
in presence of Cd2+
25
-
dibromothymoquinone
-
-
42
-
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25C, with NADH
63
-
Fe(CN)63-
-
recombinant enzyme, pH 8.2, 25C, with NADPH
3
-
Fe(III)-EDTA
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25C
3.53
-
Fe(III)-EDTA
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25C
0.15
-
Ferredoxin
-
pH 8.0, 25C
-
0.15
-
Ferredoxin
-
-
-
1
-
Ferredoxin
-
pH 8.0, 13C, mutant Y303W
-
1
-
Ferredoxin
-
-
-
2.5
-
Ferredoxin
-
pH 8.0, 13C, mutant Y308W
-
7.7
-
Ferredoxin
-
pH 8.0, 13C, mutant Y308S
-
23.9
-
Ferredoxin
-
pH 8.0, 13C, mutant Y308F
-
32
-
Ferredoxin
-
pH 8.0, 13C, mutant Y303F
-
58
-
Ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 100 mM
-
70
-
Ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 200 mM
-
90
174
Ferredoxin
-
-
-
90
-
Ferredoxin
-
native enzyme, pH 8.0, 30C
-
117
-
Ferredoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 28 mM
-
120
-
Ferredoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 200 mM
-
130
-
Ferredoxin
-
mutant lacking pH 8.2, 25C
-
135
-
Ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 200 mM
-
139
-
Ferredoxin
-
pH 8.0, 13C, wild-type enzyme
-
148
-
Ferredoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 200 mM
-
155
-
Ferredoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 100 mM
-
174
-
Ferredoxin
-
recombinant enzyme, pH 8.0, 30C
-
176
-
Ferredoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 28 mM
-
192
-
Ferredoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 100 mM
-
200
600
Ferredoxin
-
-
-
200
-
Ferredoxin
-
pH 8.0, 13C, wild-type enzyme
-
209
-
Ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 100 mM
-
225
-
Ferredoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 28 mM
-
260
-
Ferredoxin
-
wild-type, pH 8.2, 25C
-
280
-
Ferredoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 28 mM
-
45
-
ferredoxin I
-
pH 7.0, 15C, recombinant chimeric enzyme
-
82
-
ferredoxin I
-
pH 7.0, 15C, wild-type leaf isozyme
-
115
-
ferredoxin I
-
pH 7.0, 15C, wild-type root isozyme
-
177
-
ferredoxin I
-
wild-type cofactor, pH 7.5, 25C
-
32.2
-
ferredoxin II
-
wild-type cofactor, pH 7.5, 25C
-
36.8
-
ferredoxin II
-
ferredoxin mutant D64N pH 7.5, 25C
-
147
-
ferredoxin II
-
ferredoxin mutant Q39R/S28E, pH 7.5, 25C
-
0.004
-
Flavodoxin
-
flavodoxin I or II
-
0.02
-
Flavodoxin
-
pH 7.5, 37C
-
0.094
-
Flavodoxin
-
pH 7.5, 37C, in presence of FAD
-
0.158
-
Flavodoxin
-
pH 7.5, 37C, in presence of riboflavin
-
2
8
Flavodoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 200 mM
-
2.5
-
Flavodoxin
-
pH 8.0, 13C, mutant Y303W
-
4
-
Flavodoxin
-
pH 8.0, 13C, mutant Y308F
-
7
-
Flavodoxin
-
pH 8.0, 13C, mutant Y303F
-
8.3
-
Flavodoxin
-
pH 8.0, 13C, mutant Y308W
-
13.8
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57E
-
14
-
Flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 200 mM
-
14
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59E/I92E
-
15.3
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59A/I92A
-
17
-
Flavodoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 28 mM
-
19
-
Flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 100 mM
-
19
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59A
-
20
-
Flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 200 mM
-
23.3
-
Flavodoxin
-
pH 8.0, 13C, wild-type enzyme
-
23.3
-
Flavodoxin
-
using cytochrome c as electron acceptor
-
24
-
Flavodoxin
-
recombinant wild-type enzyme, pH 8.0, 25C, ionic strength of 28 mM
-
25
-
Flavodoxin
-
recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 100 mM; recombinant mutant E139Q, pH 8.0, 25C, ionic strength of 28 mM
-
25.8
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I92A
-
26
-
Flavodoxin
-
recombinant mutant E139K, pH 8.0, 25C, ionic strength of 100 mM
-
26.5
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I92E
-
27.5
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59E
-
30.6
-
Flavodoxin
-
pH 8.0, 13C, wild-type enzyme
-
38
-
Flavodoxin
-
recombinant mutant E139D, pH 8.0, 25C, ionic strength of 28 mM
-
52.7
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57R
-
90.3
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57K
-
0.0042
-
flavodoxin I
-
pH 8.0, 25C
-
0.0005
-
NADH
P21890
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
0.008
-
NADH
P21890
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
0.02
-
NADH
-
mutant T155G, pH 8.0
0.04
-
NADH
-
mutant S223D/R224Q/R233L/Y235F, pH 8.0; mutant T155G/A160T/S223D/R224Q/R233L/Y235F, pH 8.0
0.05
-
NADH
-
mutant L263P, pH 8.0
0.06
-
NADH
-
mutant T155G/S223D/R224Q/R233L/Y235F, pH 8.0
0.07
-
NADH
-
mutant T155G/A160T, pH 8.0
0.1
-
NADH
-
mutant S223D/R233L/Y235F, pH 8.0
0.13
-
NADH
-
mutant L263A, pH 8.0
0.16
-
NADH
-
wild-type enzyme, pH 8.0
0.16
-
NADH
P21890
wild type enzyme of Anabaena sp.
0.28
-
NADH
-
mutant T155G/R224Q/R233L/Y235F, pH 8.0
0.33
-
NADH
-
mutant T155G/A160T/L263P, pH 8.0
0.33
-
NADH
P21890
mutant T155G/A160T/L263P, called PP3
0.4
-
NADH
-
ferredoxin reduction, pH 7.0, 24C
0.65
-
NADH
P21890
mutant T155G/A160T/L263P/R264P/G265P, called PP5
0.86
-
NADH
-
mutant R233L/Y235F, pH 8.0
1.16
-
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
1.2
-
NADH
-
mutant R224Q/R233L/Y235F, pH 8.0
2.1
-
NADH
-
mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
3.03
-
NADH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
3.09
-
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
3.11
-
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
4.59
-
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
5.6
-
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
7.71
-
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
8.21
-
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
9.18
-
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
9.6
-
NADH
-
pH 7.0, 15C, recombinant chimeric enzyme, diaphorase activity
10
-
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
10.18
-
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
10.64
-
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
13.2
-
NADH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
16.44
-
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
17.47
-
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
19.24
-
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
31
-
NADH
P21890
mutant T155G/A160T/L263P/Y303S, called PP3CT
0.0003
-
NADPH
P21890
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
0.02
-
NADPH
-
mutant T155G/A160T/S223D/R224Q/R233L/Y235F, pH 8.0
0.03
-
NADPH
-
mutant T155G/A160T/S223D/R224Q/R233L/Y235F/L263P, pH 8.0
0.05
-
NADPH
-
mutant S223D/R224Q/R233L/Y235F, pH 8.0
0.06
-
NADPH
-
mutant T155G/S223D/R224Q/R233L/Y235F, pH 8.0
0.2
-
NADPH
-
mutant T155G/R224Q/R233L/Y235F, pH 8.0
0.24
-
NADPH
-, Q5CVU8
pH 7.4, temperature not specified in the publication, recombinant enzyme
0.6
-
NADPH
-, Q5CVU8
pH 8.2, temperature not specified in the publication, recombinant enzyme
1.3
-
NADPH
-
mutant R224Q/R233L/Y235F, pH 8.0
1.91
-
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
2.2
-
NADPH
-
wild-type, 30C, pH 8.0
3.7
-
NADPH
-
NADPH cytochrome c reductase activity, flavodoxin
3.8
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286K
3.82
-
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
4.51
-
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
4.77
-
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
5.99
-
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
6
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
6.18
-
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
6.8
-
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
7.13
-
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
7.2
-
NADPH
Q9L6V3
diaphorase activity, pH 8.0
7.5
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
7.5
-
NADPH
-
using cytochrome c as electron acceptor
7.54
-
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
10.1
-
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30C, pH 8.0
10.28
-
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
10.77
-
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
11.18
-
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
11.92
-
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
12.5
-
NADPH
-
in presence of Cd2+
17
-
NADPH
-
mutant L263P, pH 8.0
17.5
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
20.38
-
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
21.71
-
NADPH
-, Q5CVU8
pH 6.8, temperature not specified in the publication, recombinant enzyme
21.72
-
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
22
-
NADPH
-
mutant R233L/Y235F, pH 8.0
22.7
-
NADPH
-
2,6-dichlorophenolindophenol reduction, pH 7.0, 24C
23.2
-
NADPH
-
-
27
-
NADPH
-
electron transfer via the enzyme to Fe(CN)63-
35
-
NADPH
P21890
mutant T155G/A160T/L263P/R264P/G265P, called PP5
35.4
-
NADPH
-
ferredoxin reduction, pH 7.0, 24C
37.61
-
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
38.5
-
NADPH
P21890
mutant T155G/A160T/L263P/Y303S, called PP3CT
44.5
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
55
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
59
-
NADPH
-
recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
60
-
NADPH
-
mutant L263A, pH 8.0
65
-
NADPH
-
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
70
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
72
-
NADPH
-
mutant T155G/A160T, pH 8.0
73.5
-
NADPH
-
mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30C, pH 8.0
74.1
-
NADPH
-
wild-type, 30C, pH 8.0
77
-
NADPH
-
mutant T155G/A160T/L263P, pH 8.0
77
-
NADPH
P21890
mutant T155G/A160T/L263P, called PP3
81
-
NADPH
-
recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
81.5
-
NADPH
-
wild-type enzyme, pH 8.0
81.5
-
NADPH
P21890
wild type enzyme of Anabaena sp.
85
-
NADPH
-
using K3Fe(CN)6 as electron acceptor
88
-
NADPH
-
recombinant mutant E139Q, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
89
-
NADPH
-
recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25C, ionic strength of 28 mM
97
-
NADPH
-
mutant T155G, pH 8.0
100
-
NADPH
-
NADPH cytochrome c reductase activity, ferredoxin
105
-
NADPH
-
NADPH-dichlorophenol indophenol diaphorase activity
125
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor
185
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
225
520
NADPH
-
electron transfer via the enzyme to K3Fe(CN)6
225
-
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
233
-
NADPH
-
NADPH-ferredoxin-cytochrome c reductase activity
250
-
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
258
-
NADPH
-, Q8EY89
in 50 mM Tris-HCl, pH 8, at 30C
267
-
NADPH
-
diaphorase activity, FNR-flavodoxin complex
424
-
NADPH
-
mutant lacking pH 9.0, 25C
470
-
NADPH
-
wild-type
500
-
NADPH
-
pH 7.0, 15C, wild-type leaf isozyme, diaphorase activity
517
-
NADPH
-
NADPH-ferricyanide diaphorase activity
517
-
NADPH
-
diaphorase activity
520
-
NADPH
-
pH 7.0, 15C, wild-type root isozyme, diaphorase activity
520
-
NADPH
-
electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c
540
-
NADPH
-
wild-type, pH 9.0, 25C
550
-
NADPH
-
electron transfer via the enzyme to K3Fe(CN)6
560
-
NADPH
-
pH 7.0, 15C, recombinant chimeric enzyme, diaphorase activity
625
-
NADPH
-
mutant Q242R
0.15
-
oxidized ferredoxin
-
with NADPH
0.004
-
oxidized flavodoxin
-
with NADPH, any of the Escherichia coli flavodoxins
200
-
reduced ferredoxin
-
above, electron transfer via the enzyme to NADP+
600
-
reduced ferredoxin
-
electron transfer via the enzyme to NADP+
0.25
-
reduced flavodoxin
Q9L6V3
pH 8.0
0.0039
-
flavodoxin II
-
pH 8.0, 25C
-
additional information
-
additional information
-
low efficiency
-
additional information
-
additional information
-
the low efficiency is intrinsic to the reductase itself
-
additional information
-
additional information
-
low efficiency
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
76.3
-
Fe(III)-EDTA
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in the absence of free flavin, in 50 mM sodium phosphate (pH 7.0), at 25C
284630
972
-
Fe(III)-EDTA
P28861
in the presence of 0.15 mM Fe(III)-EDTA, in the presence of 0.15 mM FAD, in 50 mM sodium phosphate (pH 7.0), at 25C
284630
8000
-
Ferredoxin
-
Plasmodium falciparum ferredoxin PfFd is tested;using cytochrome c as electron acceptor
0
200
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57E
0
350
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59E/I92E
0
450
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59A/I92A
0
690
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57R
0
700
-
Flavodoxin
-
using cytochrome c as electron acceptor
0
1010
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant W57K
0
2380
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59A
0
2770
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I92E
0
3090
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I59E
0
3150
-
Flavodoxin
-
using cytochrome c as electron acceptor, for mutant I92A
0
0.0004
-
NADH
P21890
mutant T155G/A160T/S223D/Y235F/L263P/R264P/G265P, called AMP2PP5
14331
0.006
-
NADH
P21890
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
14331
0.2
-
NADH
P21890
wild type enzyme of Anabaena sp.
14331
0.8
-
NADH
P21890
mutant T155G/A160T/L263P, called PP3
14331
1.4
-
NADH
P21890
mutant T155G/A160T/L263P/R264P/G265P, called PP5
14331
30
-
NADH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
14331
70
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
14331
90
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor; for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
14331
110
-
NADH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
14331
110
-
NADH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
14331
130
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
14331
170
-
NADH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
14331
540
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
14331
550
-
NADH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
14331
680
-
NADH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
14331
800
-
NADH
P21890
mutant T155G/A160T/L263P/Y303S, called PP3CT
14331
860
-
NADH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
14331
930
-
NADH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
14331
1060
-
NADH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor; for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
14331
1170
-
NADH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
14331
1860
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
14331
2690
-
NADH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
14331
2870
-
NADH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
14331
3130
-
NADH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
14331
3270
-
NADH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
14331
4630
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
14331
6730
-
NADH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
14331
7090
-
NADH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
14331
0.000000064
-
NADPH
-, Q5CVU8
pH 7.4, 25C, recombinant enzyme; pH 8.2, 25C, recombinant enzyme
27498
0.0000009
-
NADPH
-, Q5CVU8
pH 6.8, 25C, recombinant enzyme
27498
0.0002
-
NADPH
P21890
mutant T155G/A160T/S223D/L263P/R264P/G265P, called AMP1PP5
27498
20
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286L
27498
45
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286K
27498
49
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286A
27498
85
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286A
27498
90
-
NADPH
-
for FprB in a flavin free assay, using Fe(III)-EDTA as electron acceptor
27498
530
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
27498
720
-
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
27498
750
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor
27498
770
-
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
27498
770
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdB as electron acceptor
27498
840
-
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor
27498
930
-
NADPH
-
for FprB with FAD as cofactor, using Fe(III)-citrate as electron acceptor
27498
1000
-
NADPH
-
for FprA in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
27498
1130
-
NADPH
-
for FprB in a flavin free assay, using K3Fe(CN)6 as electron acceptor
27498
1140
-
NADPH
-
for FprB in a flavin free assay, using 2,6-dichlorophenolindophenol as electron acceptor
27498
1190
-
NADPH
-
for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor
27498
1200
-
NADPH
-
using cytochrome c as electron acceptor
27498
1300
-
NADPH
-
using 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloride as electron acceptor
27498
1320
-
NADPH
-
for FprA in a flavin free assay, using Fe(III)-EDTA as electron acceptor
27498
1370
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
27498
1500
-
NADPH
P21890
mutant T155G/A160T/L263P/R264P/G265P, called PP5
27498
1570
-
NADPH
-
for FprA in a flavin free assay, using Fe(III)-citrate as electron acceptor
27498
1680
-
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-EDTA as electron acceptor
27498
2090
-
NADPH
-
for FprB in a flavin free assay, using Fe(III)-citrate as electron acceptor
27498
3050
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
27498
3150
-
NADPH
-
in an assay using 2,6-dichlorophenolindophenol as electron acceptor for mutant H286Q
27498
3230
-
NADPH
-
for FprA in a flavin free assay, using K3Fe(CN)6 as electron acceptor
27498
3300
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor for mutant H286Q
27498
3500
-
NADPH
-
in an assay using K3Fe(CN)6 as electron acceptor
27498
3720
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
27498
4590
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [4Fe-4S]-ferredoxin FdxA as electron acceptor
27498
6040
-
NADPH
-
for FprA with FMN as cofactor, using Fe(III)-citrate as electron acceptor
27498
6400
-
NADPH
P21890
mutant T155G/A160T/L263P, called PP3
27498
8500
-
NADPH
-
using K3Fe(CN)6 as electron acceptor
27498
9400
-
NADPH
P21890
mutant T155G/A160T/L263P/Y303S, called PP3CT
27498
11000
-
NADPH
-
for FprB in a cytochrome c assay, using Pseudomonas putida [2Fe-2S]-ferredoxin FdA as electron acceptor
27498
11510
-
NADPH
-
for FprA in a cytochrome c assay, using Pseudomonas putida flavodoxin Fld as electron acceptor
27498
13500
-
NADPH
P21890
wild type enzyme of Anabaena sp.
27498
17000
-
NADPH
-
for FprB with FMN as cofactor, using Fe(III)-citrate as electron acceptor
27498
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.024
-
2'-AMP
-
when 2,6-dichlorophenolindophenol serves as electron acceptor
1.72
-
Cd2+
-
pH 8.7, temperature not specified in the publication
0.05
0.1
Ferredoxin
-
pH 8.0, 25C
-
0.185
-
ferricyanide
-
25C, pH 8.2, cosubstrate NADH
0.23
-
ferricyanide
-
25C, pH 8.2, cosubstrate NADPH
0.05
0.1
flavodoxin I, flavodoxin II
-
pH 8.0, 25C
-
0.23
-
K3Fe(CN)6
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.73
-
-
NADPH/2,6-dichlorphenol indophenol diaphorase activity
1.05
-
-
electron donor NADH, cofactor FAD
2.58
-
-
electron donor NADPH, cofactor FAD
5.47
-
-
electron donor NADH, cofactor FMN
5.73
-
-
electron donor NADPH, cofactor FMN
9.255
-
-
cytochrome c reduction
9.4
-
-
fraction 1
11
-
Q93RE3
purified 45 kDa enzyme form, substrate 2,6-dichlorophenolindophenol, 22C
16.3
-
-
reduction of cytochrome c
21.2
-
-
Vmax value is 28 micromol/min/mg when NADPH is used as the electron donor, Vmax value is 22 micromol/min/mg when reduced ferredoxin Fd1 is used as the electron donor and NADP+ as electron acceptor
25
-
A0ZSY5
ferredoxin-dependent activity at pH 9.5
28
-
-
fraction 4
30
-
-
ferredoxin-dependent activity at pH 10
33.8
-
-
purified enzyme
39.4
-
-
fraction 2
53.9
-
-
fraction 3
60
-
-
quinone-dependent activity at pH 7.5
60
-
A0ZSY5
quinone-dependent activity at pH 7.5
70
-
-
ferredoxin-dependent activity at pH 6.5
76
-
-
diaphorase activity of the 32 kDa enzyme
77
-
A0ZSY5
-
79
-
-
diaphorase activity of the 35 kDa enzyme
95
-
-
ferredoxin-dependent activity at pH 7
110
-
A0ZSY5
ferredoxin-dependent activity at pH 6.5
120
-
-
-
128
-
-
NADPH/cytochrome c activity
140
-
A0ZSY5
ferredoxin-dependent activity at pH 7
160.8
-
-
fusion protein with GST, ferricyanide reduction
260
-
-
quinone-dependent activity at pH 10
280
-
-
quinone-dependent activity at pH 9.7
325
-
A0ZSY5
quinone-dependent activity at pH 10
400
-
A0ZSY5
quinone-dependent activity at pH 9.7
478.6
-
Q8RVZ8, Q8RVZ9
crude extract; crude extract
11110
-
Q8RVZ8, Q8RVZ9
after 501.79fold purification; after 501.79fold purification
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activity of wild-type and mutant enzymes with different cofactors
additional information
-
Q93RE3
-
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
8
-
assay at
6.8
-
-, Q5CVU8
-
7
-
-
reduced ferredoxin + NADP+
7
-
-
assay at
7
-
-
assay at
7
-
-
in a ferredoxin-dependent cytochrome c reduction assay
7
-
A0ZSY5
in a ferredoxin-dependent cytochrome c reduction assay
7
-
O05268
assay at
7.1
-
-
ferredoxin dependent cytochrome c reducing activity
7.4
7.8
-
ferredoxin-dependent cytochrome c reductase activity
7.5
-
-
-
7.5
-
-
assay at, ferric reductase activity
7.5
-
-
assay at
7.5
-
-
assay at
7.5
-
Q96YN9, -
assay at
7.9
-
-
NADP+ photoreduction activity
8
-
-
cytochrome c reduction
8
-
-
assay at, steady-state kinetics
8
-
-
diaphorase activity assay at
8
-
-
assay at
8
-
Q9L6V3
assay at
8
-
-
assay at
8
-
-
assay at
8
-
Q93RE3
assay at
8
-
-
assay at
8.2
-
-
assay at, diaphorase activity
8.4
-
-
100 mM Tris-HCl
8.9
-
-
NADPH-NAD+ transhydrogenase
9
-
-
diaphorase activity at 55C
9
-
-
diaphorase activity decreases at lower pH
9.4
-
-
at 25C, diaphorase activity is largely independent of pH, slight optimum at pH 9.3
9.5
-
-
diaphorase activity
9.7
-
-
in a 2,6-dichlorophenolindophenol reduction assay; in a quinone-dependent cytochrome c reduction assay
9.7
-
A0ZSY5
in a 2,6-dichlorophenolindophenol reduction assay; in a quinone-dependent cytochrome c reduction assay
10
-
-
NADPH + methyl viologen
10
-
-
diaphorase activity
10.1
-
-
NADPH-2,6-dichlorophenol-indophenol diaphorase activity
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
10
-
ferredoxin-dependent activity at pH 6.5 is 70 micromol/min/mg, at pH 7 is 95 micromol/min/mg and at pH 10 is 30 micromol/min/mg
6.5
9.5
A0ZSY5
ferredoxin-dependent activity at pH 6.5 is 110 micromol/min/mg, at pH 7 is 140 micromol/min/mg and at pH 9.5is 25 micromol/min/mg
6.8
8.2
-, Q5CVU8
assay range
7.5
10
-
quinone-dependent activity at pH 7.5 is 60 micromol/min/mg, at pH 9.7 is 280 micromol/min/mg and at pH 10 is 260 micromol/min/mg
7.5
10
A0ZSY5
quinone-dependent activity at pH 7.5 is 60 micromol/min/mg, at pH 9.7 is 400 micromol/min/mg and at pH 10 is 325 micromol/min/mg
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
15
-
-
assay at
24
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-
assay at
25
-
-, Q5CVU8
assay at
25
-
O05268
assay at
40
-
-
in a 2,6-dichlorophenolindophenol reduction assay; in a ferredoxin-dependent cytochrome c reduction assay
45
-
-
in a quinone-dependent cytochrome c reduction assay
50
-
A0ZSY5
in a ferredoxin-dependent cytochrome c reduction assay
55
-
A0ZSY5
in a 2,6-dichlorophenolindophenol reduction assay; in a quinone-dependent cytochrome c reduction assay
60
-
-
cytochrome c reductase and diaphorase activity
80
-
Q96YN9, -
assay at
additional information
-
-
enzyme thermal inactivation is irreversible
additional information
-
Q93RE3
temperature dependence, overview
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
70
Q93RE3
activity at 52C is 3fold higher than activity at 25C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.8
5.5
Q8RVZ8, Q8RVZ9
isoelectric focusing; isoelectric focusing, isozymes FNR-A and FNR-B
5.3
5.5
Q8RVZ8, Q8RVZ9
isozyme FNRII
5.5
-
Q9SLP6
isozyme FNRI
5.54
-
F4JZ46, Q8W493
mature FNRII
5.8
-
-
native and recombinant enzyme, isoelectric focusing
5.9
6.2
Q8RVZ8, Q8RVZ9
isozyme FNRI
6.19
-
F4JZ46, Q8W493
mature FNRI
6.76
-
Q9SLP6
isozyme FNRI
additional information
-
Q8RVZ8, Q8RVZ9
isoelectric focusing of isozymes, overview; isoelectric focusing of isozymes, overview
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
high- or low-CO2-grown (H or L)-cells
Manually annotated by BRENDA team
Synechocystis sp. 6803
-
high- or low-CO2-grown (H or L)-cells
-
Manually annotated by BRENDA team
-
photosynthetic leaf isozyme
Manually annotated by BRENDA team
Q8RVZ8, Q8RVZ9
;
Manually annotated by BRENDA team
-
isozyme L-FNR I
Manually annotated by BRENDA team
Q8RVZ8, Q8RVZ9
four distinct leaf FNR isoforms, two in each group, FNRI and FNRII; four distinct leaf FNR isoforms, two in each group, FNRI and FNRII
Manually annotated by BRENDA team
Q8RVZ8, Q8RVZ9
primary wheat leaf; primary wheat leaf
Manually annotated by BRENDA team
-
leaf-type, or chloroplast, or photosynthetic LFNR
Manually annotated by BRENDA team
Spinacia oleracea Atlanta
-
-
-
Manually annotated by BRENDA team
Triticum aestivum Paragon
-
primary wheat leaf; primary wheat leaf
-
Manually annotated by BRENDA team
-
nonphotosynthetic root isozyme
Manually annotated by BRENDA team
F4JZ46, Q8W493
both FNR chloroplast isozyme genes are predominantly expressed in the rosette leaves; both FNR chloroplast isozyme genes are predominantly expressed in the rosette leaves
Manually annotated by BRENDA team
Cryptosporidium parvum IOWA-1
-
-
-
Manually annotated by BRENDA team
-
non-photosynthetic plant tissue
Manually annotated by BRENDA team
additional information
F4JZ46, Q8W493
only minor amount of chloroplast isozyme FNR1 mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue; only minor amount of chloroplast isozyme FNR mRNA are detected in the stems, flowers and siliques. Chloroplast FNR transcripts or FNR proteins are not detected in the root tissue
Manually annotated by BRENDA team
additional information
-, Q5CVU8
CpmtFd and CpmtFNR genes are constitutively transcribed during the complex parasite life cycle, real-time quantitative RT-PCR expression analysis, overview
Manually annotated by BRENDA team
additional information
Cryptosporidium parvum IOWA-1
-
CpmtFd and CpmtFNR genes are constitutively transcribed during the complex parasite life cycle, real-time quantitative RT-PCR expression analysis, overview
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
; active NADPH-enzyme-ferredoxin cascade
Manually annotated by BRENDA team
-
associated to the grana fraction
Manually annotated by BRENDA team
-
distribution between thylakoid membranes and chloroplast stroma in Nicotiana tabacum. Thylakoids of transgenic plants with 5fold increase in enzyme protein show only about 20% increase in electron transport from water to NADP+. transgenic plants fail to show significant differences in CO2 assimilation rates but show enhanced tolerance to photooxidative damage and redox-cycling herbicides
Manually annotated by BRENDA team
F4JZ46, Q8W493
isozyme FNRII is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview; isozyme FNRI is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview
Manually annotated by BRENDA team
Q8RVZ8, Q8RVZ9
the enzyme is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview; the enzyme is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview
Manually annotated by BRENDA team
Q9SLP6
the enzyme is targeted to the chloroplasts. The two chloroplast proteins, Tic62 and TROL, form high molecular weight protein complexes with FNR at the thylakoid membrane, and thus seem to act as the long-sought molecular anchors of FNR to the thylakoid membrane, overview
Manually annotated by BRENDA team
Q8RVZ8, Q8RVZ9
subchloroplast localization of pFNR isoforms, overview. Isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD shows an eual distribution between stroma and thylakoid; subchloroplast localization of pFNR isoforms, overview. Isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS shows a differential distribution between stroma and thylakoid with 76% of pFNRISKKQ and only 33% of pFNRIKKVS located in the thylakoid pool
Manually annotated by BRENDA team
-
FNR is a soluble protein associated with thylakoid membranes
Manually annotated by BRENDA team
-
FNR occurs in stroma, at the inner envelope membrane, and bound to thylakoid membranes. Tic62 and TROL complexes are responsible for the major part of the thylakoid-bound pool of FNR
Manually annotated by BRENDA team
-
FNR occurs in stroma and bound to thylakoid membranes
Manually annotated by BRENDA team
Spinacia oleracea Atlanta
-
-
-
Manually annotated by BRENDA team
Triticum aestivum Paragon
-
subchloroplast localization of pFNR isoforms, overview. Isozyme FNRII with subforms pFNRIIISKK and pFNRIIKKQD shows an eual distribution between stroma and thylakoid; subchloroplast localization of pFNR isoforms, overview. Isozyme FNRI with subforms pFNRISKKQ and pFNRIKKVS shows a differential distribution between stroma and thylakoid with 76% of pFNRISKKQ and only 33% of pFNRIKKVS located in the thylakoid pool
-
Manually annotated by BRENDA team
-
enzyme is bound to phycobilisomes via the N-terminal enzyme domain to the peripheral rods of the phycobilisome, average value of 1.3 molecules of enzyme per phycobilisome, structure modeling, interaction analysis
Manually annotated by BRENDA team
Arthrospira platensis IAM M-135
-
-
-
Manually annotated by BRENDA team
Q9SLP6
-
-
Manually annotated by BRENDA team
Rhodobacter capsulatus 37b4
-
-
-
-
Manually annotated by BRENDA team
Q8W493, Q9FKW6
;
-
Manually annotated by BRENDA team
-
tightly bound or loosely bound on the outer surface, 2 enzyme pools
Manually annotated by BRENDA team
-
the enzyme is associated with the stromal side of the thylakoid membrane in the chloroplast
Manually annotated by BRENDA team
Q8RVZ8, Q8RVZ9
the enzyme is associated with the stromal side of the thylakoid membrane in the chloroplast; the enzyme is associated with the stromal side of the thylakoid membrane in the chloroplast
Manually annotated by BRENDA team
Q8W493, Q9FKW6
In Arabidopsis thaliana, FNR1 is essential for the binding of FNR to the thylakoid membrane, hence in FNR1-lacking plant lines FNR2 can only be found in stroma.; In Arabidopsis thaliana, FNR1 is essential for the binding of FNR to the thylakoid membrane, hence in FNR1-lacking plant lines FNR2 can only be found in stroma.
Manually annotated by BRENDA team
-
FNR is a soluble protein associated with thylakoid membranes
Manually annotated by BRENDA team
Arthrospira platensis IAM M-135, Synechocystis sp. 6803
-
-
-
Manually annotated by BRENDA team
Cryptosporidium parvum IOWA-1
-
mtFNR
-
Manually annotated by BRENDA team
additional information
-
nucleus-encoded enzyme
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Bacillus subtilis (strain 168)
Bacillus subtilis (strain 168)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Burkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301)
Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Nostoc sp. (strain ATCC 29151 / PCC 7119)
Plasmodium falciparum (isolate 3D7)
Plasmodium falciparum (isolate 3D7)
Plasmodium falciparum (isolate 3D7)
Plasmodium falciparum (isolate 3D7)
Plasmodium falciparum (isolate 3D7)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pseudomonas sp. (strain KKS102)
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Xanthomonas axonopodis pv. citri (strain 306)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24600
-
-
gel filtration
27000
-
-
SDS-PAGE
28000
-
-
gel filtration
28600
-
-
calculated from amino acid sequence
29000
-
-
SDS-PAGE, purified enzyme
30000
-
Q9L6V3
about, gel filtration
31000
-
-
truncated form after limited proteolysis with proteases, deletion of N-terminal region
31500
-
-
strain MAC, sedimentation equilibrium
31970
-
-
calculated from amino acid composition, enzyme I
32000
-
-
lack of the first 28 amino acid residues after expression in Escherichia coli
32240
-
-
calculated from amino acid composition, enzyme II
33000
35000
-
gel filtration, SDS-PAGE
33000
36000
-
ultracentrifugation
33000
38000
-
strain 7119, multiple forms
33000
-
-
gel filtration and SDS-PAGE, ultracentrifugation
33000
-
-
SDS-PAGE
33000
-
A0ZSY5
SDS-PAGE
33180
-
-, Q9M4D2
mature protein calculated from amino acid sequence
33300
37000
-
SDS-PAGE, gel filtration, monomer
33500
42000
-
multiple forms: a, b, c, d, e, SDS-PAGE, disc gel electrophoresis
33800
-
-
gel filtration
34000
-
-
more intense band of two bands after SDS-PAGE
34000
-
-
SDS-PAGE, monomer
34000
-
A0ZSY5
gel filtration
34140
-
-
amino acid sequence
34290
-
Q8RVZ8, Q8RVZ9
FNR-A, ESI mass spectrometry
34300
-
Q8RVZ8, Q8RVZ9
FNR-A, gel filtration
35000
-
-
after expression in E. coli
35000
-
-
gel filtration
35000
-
-
native reductase, SDS-PAGE
35000
-
-
limited proteolysis to 33 kDa is suppressed by pH 9.3
35000
-
-
native PAGE
35000
-
-
Sephacryl S-200 gel filtration, native enzyme
35000
-
Q8RVZ8, Q8RVZ9
FNR-A, SDS-PAGE
35000
-
Q8W493, Q9FKW6
SDS-PAGE; SDS-PAGE
35440
-
Q8RVZ8, Q8RVZ9
FNR-B, ESI mass spectrometry
35500
-
Q8RVZ8, Q8RVZ9
FNR-B, gel filtration
36000
-
-
at least 5 molecular forms
36000
-
-
SDS-PAGE
36000
-
-
SDS-PAGE
36000
-
-
-
36000
-
-
SDS-PAGE
36000
-
Q8RVZ8, Q8RVZ9
FNR-B, SDS-PAGE
36500
-
-
native enzyme, gel filtration
37000
-
-
SDS-PAGE, Western blot
37000
-
-
SDS-PAGE
37270
-
-
calculated from amino acid sequence
37500
-
-
native enzyme, native PAGE
37600
-
-
gel filtration, mutant lacking amino acids 81 to 118
38000
-
-
gel filtration, monomer
38000
-
-
SDS-PAGE
38000
-
-
gel filtration, monomer
38500
-
-
recombinant enzyme, gel filtration
38600
-
-
SDS-PAGE
39000
-
-
glutaraldehyde crosslinking
40000
-
-
SDS-PAGE
40410
-
-, Q9M4D2
calculated molecular mass from amino acid analysis of FNR including amino-terminal transit peptide
42000
-
-
recombinant nezyme, native PAGE
45000
-
-
gel filtration
46000
-
-
SDS-PAGE
46300
-
-
gel filtration, wildtype
47000
-
-
gel filtration
48000
-
-
SDS-PAGE
49000
-
-
predicted according to protein sequence
50000
-
-
gel filtration, P-2
50320
-
-
calculated from cDNA sequence
51000
-
-
SDS-PAGE
51500
-
-
gel filtration
52000
-
-
minimum MW, SDS-PAGE
52000
-
-
weaker band of two bands after SDS-PAGE
52000
-
-
gel filtration, SDS-PAGE
52300
-
-
calculated from amino acid analysis
53000
-
-
recombinant enzyme, gel filtration
60000
-
-
gel filtration
60000
-
-
fusion protein with glutathione S-transferase
70000
-
-
SDS-PAGE, dimer
70000
-
-
SDS-PAGE, dimer
72000
-
-
SDS-PAGE
80000
-
-
gel filtration
80000
-
-
SDS-PAGE, occurs in higher concentrations when enzyme is purified with protease inhibitors
90000
-
-
gel filtration
90000
-
-
NaCl solubilized FNR from Spirulina platensis thylakoid membranes contained the 46000 Da FNR and a 17000 Da protein
94000
-
-
gel filtration
117000
-
-
gel filtration, P-1
additional information
-
-
-
additional information
-
-
-
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 38000, recombinant N-terminally truncated enzyme, SDS-PAGE, 1 * 34000, chloroplast enzyme form, SDS-PAGE
?
Q93RE3
x * 43415, amino acid sequence calculation, x * 45000, active enzyme form containing the CpcD-like domain, SDS-PAGE, x * 34000, enzyme form lacking the CpcD-like domain, SDS-PAGE, x * 78000, enzyme in complex with phycocyanin, SDS-PAGE
?
Q55318
x * 34000, isoform FNRS, x * 46000, isoform FNRL
?
-
x * 35000, SDS-PAGE
?
P28861
x * 28000, SDS-PAGE; x * 28981, calculated from amino acid sequence
?
Synechocystis sp. PCC6803
-
x * 34000, isoform FNRS, x * 46000, isoform FNRL
-
dimer
-
composed of two different subunits, 1 * 15000 + 1* 36000, SDS-PAGE
dimer
-
two different subunits, SDS-PAGE, occurs in higher concentrations when enzyme is purified with protease inhibitors
dimer
-
2 * 40000, SDS-PAGE
dimer
-
the enzyme undergoes NADP+-dependent dimerization (inactive enzyme form)
dimer
Anabaena sp. 7119
-
two different subunits, SDS-PAGE, occurs in higher concentrations when enzyme is purified with protease inhibitors
-
heterodimer
-
LFNR1 is essential for the membrane attachment of LFNR2, strongly indicating the formation of a heterodimer
homodimer
-
2 * 45000, gel filtration
homodimer
Q96YN9, -
2 * 36600, calculated from sequence
homodimer
Chlorobaculum tepidum CT1512
-
2 * 45000, gel filtration
-
homodimer
Sulfolobus tokodaii 7
-
2 * 36600, calculated from sequence
-
monomer
-
1 * 38000 gel filtration
monomer
-
1 * 50000, recombinant enzyme, SDS-PAGE
monomer
Q9L6V3
1 * 30000, about, recombinant and native enzyme, SDS-PAGE
monomer
-
1 * 35000, SDS-PAGE
monomer
-
1 * 39000, wild-type, calculated, 1 * 35000, mutant lacking amino acids 81 to 118
monomer
-
1 * 28000, gel filtration
monomer
-, Q8EY89
X-ray scattering
monomer
-
1 * 35000, Sephacryl S-200 gel filtration, native enzyme
monomer
-
1 * 24600, gel filtration
monomer
-
1 * 27000, fast protein liquid chromatography
monomer
-
1 * 47000, gel filtration
monomer
A0ZSY5
1 * 34000, gel filtration
monomer
-
1 * 45000, gel filtration, 1 * 39000 glutaraldehyde crosslinking, the difference is due to stabilization of native enzyme in a relatively open conformation, therefore a molecular dimension larger than that of globular proteins of similar mass is observable
monomer
Arthrospira platensis IAM M-135
-
1 * 47000, gel filtration
-
monomer
-
1 * 24600, gel filtration
-
monomer
Rhodobacter capsulatus 37b4
-
1 * 30000, about, recombinant and native enzyme, SDS-PAGE
-
additional information
-
3-domain-structure
additional information
-
2-domain structure, structure analysis
additional information
-
2-domain structure
additional information
-
2-domain structure, structure analysis
additional information
-
2-domain structure
additional information
-
2-domain structure, structure analysis
additional information
-
enzyme forms aggregates in solution which can be prevented by addition of 10% glycerol and 2-mercaptoethanol
additional information
-
three-dimensional structure of mutant E139K
additional information
-
three-dimensional structure analysis, intramolecular stabilization and stabilizationof enzyme-substrate complex, overview
additional information
-
three-dimensional structure analysis, overview
additional information
-
three-dimensional structure determination and analysis, overview
additional information
-
a flexible N-terminal region of enzyme contributes to interaction with ferredoxin. The nicotinamide moiety of NADP+ is accessible to the C-terminal Y314
additional information
-
study on enzyme conformation by limited proteolysis. Protein substrate ferredoxin protects ferredoxin-NADP+ reductase against cleavage both at its N-terminal peptide and at its largest sequence insertion of 28 residues
additional information
-
study on structural stability and dynamics of protein by H/D exchange at pD values of 6.0 and 8.0 corresponding to physiological conditions in the chloroplast. Highly protected regions of protein match well with the hydrophobic cores suggested from the crystal structure. The NADP+-binding domain can be divided into two subdomains
additional information
-
Under oxidizing conditions, Plasmodium falciparum FNR constitutes an inactive dimeric form stabilized by an intermolecular disulfide bond. Monomer-dimer interconversion can be controlled by oxidizing and reducing agents that are possibly present within the apicoplast, such as H2O2, glutathione, and lipoate.
additional information
F4JZ46, Q8W493
chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview; chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview
additional information
Q8RVZ8, Q8RVZ9
chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview; chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview
additional information
Q9SLP6
chloroplast FNR isozymes are hydrophilic proteins with a molecular weight of approximately 35 kDa. Structure of FNR in complex with ferredoxin, overview
additional information
Q8RVZ8, Q8RVZ9
three-dimensional modelling of pFNR protein structure, overview; three-dimensional modelling of pFNR protein structure, overview
additional information
-
FNR-membrane recruitment motif, FNR-MRM, forms a polyproline helix that interacts with a proline recognition domain on FNR. FNR displays a pH-dependent high affinity to the MRM, loop residues contribute to multiple interactions with both FNR subunits
additional information
-, Q5CVU8
the mtFNR enzymatic region contains at least six highly conserved domains or motifs, including three FAD-diphosphate binding and one NADP+-diphosphate binding motifs
additional information
O05268
structure, primary sequence and oligomeric conformation, comparisons, overview
additional information
Anabaena sp. PCC7119
-
2-domain structure, structure analysis
-
additional information
Cryptosporidium parvum IOWA-1
-
the mtFNR enzymatic region contains at least six highly conserved domains or motifs, including three FAD-diphosphate binding and one NADP+-diphosphate binding motifs
-
additional information
Triticum aestivum Paragon
-
three-dimensional modelling of pFNR protein structure, overview; three-dimensional modelling of pFNR protein structure, overview
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
side-chain modification
-
the native enzyme is posttranslationally trimethylated at lysine residues K83, K89, and K135 inducing changes in the tertiary enzyme structure
proteolytic modification
Q8MTY0, -
presence of a 31 amino acid N-terminal transit peptide that may target the enzyme to mitochondria in mammal cells
proteolytic modification
Q93RE3
dissociation of the enzyme-phycocyanin complex induces the specific proteolysis between the CpcD-like domain and the FAD-binding domain to give rise to the 34 kDa enzyme form
phosphoprotein
Q8RVZ8, Q8RVZ9
the four pFNR protein isoforms are each present in the chloroplast in phosphorylated and nonphosphorylated states. The pFNR isoforms vary in putative phosphorylation responses to physiological parameters, prediction of phosphorylation sites, e.g. S75, and differences between isoforms in putative phosphorylation patterns, overview; the four pFNR protein isoforms are each present in the chloroplast in phosphorylated and nonphosphorylated states. The pFNR isoforms vary in putative phosphorylation responses to physiological parameters, prediction of phosphorylation sites, e.g. T104 and T293, and differences between isoforms in putative phosphorylation patterns, overview
phosphoprotein
Triticum aestivum Paragon
-
the four pFNR protein isoforms are each present in the chloroplast in phosphorylated and nonphosphorylated states. The pFNR isoforms vary in putative phosphorylation responses to physiological parameters, prediction of phosphorylation sites, e.g. S75, and differences between isoforms in putative phosphorylation patterns, overview; the four pFNR protein isoforms are each present in the chloroplast in phosphorylated and nonphosphorylated states. The pFNR isoforms vary in putative phosphorylation responses to physiological parameters, prediction of phosphorylation sites, e.g. T104 and T293, and differences between isoforms in putative phosphorylation patterns, overview
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme complexed with NADP+, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
Interactions between FNR and the putative protein partners, ferredoxin Fd and flavodoxin Fld, were modeled, using surface energy analysis, computational rigid-body docking simulations, and interface side-chain refinement. The results suggest the existence of alternative binding modes in these electron transfer proteins.
-
model of enzyme:flavodoxin complex based on crystal structures. Key participation of residues K75 and K72 in complex formation with both ferredoxin and flavodoxin
-
mutant
-
purified recombinant mutant E139K, hanging drop vapour diffusion method, 0.002 ml protein solution containing 0.75 mM protein in 10 mM Tris-HCl, pH 8.0, plus 0.001 ml reservoir solution containing 5% w/v beta-octylglycoside, 18% PEG 6000, 20 mM ammonium sulfate, and 0.1 M MES/NaOH, pH 5.5, equilibration against 1 ml reservoir solution at 20C, phase separation due to detergent, X-ray diffraction structure determination and analysis at 2.5 A resolution
-
purified recombinant mutant enzymes L263P, T155G/A160T, and T155G/A160T/L263P, hanging drop method, 0.002 ml of protein solution, containing 0.75 mM protein, 10 mM Tris-HCl, pH 8.0, plus 0.001 ml of unbuffered 5% w/v beta-octyl-glycoside solution, plus 0.002 ml reservoir solution, containing 18-20% w/v PEG 6000, 20 mM ammonium sulfate, 0.1 M MES-NaOH, pH 5.0, equilibration against 1 ml reservoir solution at 20C, 1-7 days, phase separation caused by detergent, X-ray diffraction structure determination and analysis at 1.63-2.15
-
crystallizations of wild-type enzyme, oxidized, or substrate-complexed, and of diverse enzyme mutants, crystal structure determination and analysis at 1.6-2.5 A resolution, overview
-
FNR in complex with NADP+, two different crystal forms, mixing of 0.001 ml of 10 mg/ml protein and 2.5 mM NADP+ with 0.001 ml of reservoir solution containing 0.1 M HEPES buffer, pH 7.5, 30% 1,2-propanediol, and 20% PEG 400 for form I, and 20% PEG 3350, 0.2 M sodium fluoride, and 5% trehalose for form II, 20C, X-ray diffraction structure determination and analysis at 1.8-1.9 A resolution, respetively, molecular replacement
O05268
purified recombinant FNR in complex with NADP+ in two different forms, 0.001 ml of 10 mg/ml protein in 50 mM Tris-HCl pH 8.0, 200 mM NaCl, and 2.5 mM NADP+, is mixed with 0.001 ml reservoir solution, 20C. The reservoir solutions consist of 0.1 M HEPES buffer pH 7.5, 30% 1,2-propanediol, 20% PEG 400 for form I, and of 20% PEG 3350, 0.2 M sodium fluoride and 5% trehalose for form II. X-ray diffraction structure determination and analysis at 1.8 and 1.9 A resolution, respectively, molecular replacement, modelling
-
-
-, Q9M4D2
crystal structure determination and analysis at 2.5 A resolution
-
hanging drop vapour diffusion method, using 0.1 M MES buffer pH 5.8 containing 16% (w/v) PEG 6K and 0.1 M ammonium sulfate as precipitant
-
diffraction to 2.4 A, space group P21
-
using 27% PEG 3350, 50 mM Tris-HCl buffer pH 7.0, at 18C
-, Q8EY89
analysis of the enzyme in complex with a synthetic peptide representing the first FNR-binding repeat from Pisum sativum Tic62, including the strictly conserved core motif KTEQPLSPYTAYDDLKPPSSPSPTKPS, based on the crystal structure PDB ID 1QG0, X-ray diffraction structure analysis at 1.7 A resolution, molecular replacement
-
crystallizations of wild-type enzyme, ferredoxin-complexed enzyme, and enzyme mutants Y308S, complexed with NADP+ or NADPH, and Y308W, complexed with NADP+, crystal structure determinations and analysis at 1.7-2.5 A resolution, overview
-
free enzyme and in complex with 2-phospho-AMP. Structures reveal a covalent dimer, which relies on the oxidation of residue C99 in two opposing subunits, and a helix-coil transition that occurs in the NADP-binding domain, triggered by 2-phospho-AMP binding. Studies in solution show that NADP+, as well as 2-phospho-AMP, promotes the formation of the disulfide-stabilized dimer. The dimer is inactive, but full activity is recovered upon disulfide reduction; in free form and in complex with 2'-phospho-AMP, in 22-25% PEG 4000, 0.1 M sodium cacodylate (pH 6.0), 0.2 M sodium acetate
-
space group P21
-
hanging drop vapour diffusion method, in 200 mM ammonium acetate, 100 mM sodium citrate tribasic dihydrate, and 25% (v/v) PEG-4000 (pH 5.6)
-
recombinant enzyme, hanging drop vapour diffusion method in presence of n-heptyl-beta-D-thioglucoside which is required for stabilization of the disordered regions of the protein, 18C, X-ray diffraction structure determination and analysis, at 1.8 A resolution
-
crystallizations of oxidized enzyme, dithionite-reduced enzyme, 2',5'-ADP-complexed enzyme, enzyme mutants S96V, E312A, E312L, and E312Q, crystal structure determinations and analysis at 1.7-2.0 A resolution, overview
-
homology modeling of wild-type and mutant S267R in complex with ferredoxin. Mutant shows major sterical and electrostatical effects on the FAD function as well as on residues Y266, I268 and Y497 neighbouring the mutation
-
crystal structure determination and analysis of leaf enzyme, free or complexed with ferredoxin, and root enzyme at 2.2-2.6 and 1.7 A resolution, respectively
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
7.5
-
reduced thermal inactivation rate at this pH-range
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
inactivation of the enzyme due to irreversible protein unfolding and dissociation of the FADH2 cofactor, slower process with binding of ferredoxin, FAD, or flavodoxin, best by riboflavin, overview
41
-
-
inactivation of the reduced enzyme
55
-
-
recombinant chimeric enzyme is slightly less stable than the wild-type parent isozymes
65
-
-
no loss of activity at 65C after incubation for 5 min
66
-
-
inactivation of the oxidized enzyme
70
-
Q93RE3
5 min, completely stable
76
-
-
50% loss of activity after 5 min
80
-
Q93RE3
5 min, loss of 60% activity
85
-
Q93RE3
5 min, inactivation
additional information
-
-
rapid thermal inactivation of reduced enzyme
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
binding of ferredoxin, FAD, flavodoxin, or riboflavin stabilizes the enzyme
-
instability
-
interaction with Tic62 stabilizes FNR
-
complex formation with phycocyanin via the CpcD-like domain stabilizes the enzyme
Q93RE3
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, rapid loss of activity
-
-20C, stable for 2 months in nitrogen or in air
-
4C, stable for 1 week at 4C when bound to ADP-agarose column
-
-30C, aggregation of the 45 kDa enzyme form occurs during storage, 50% loss of activity after 1 week
Q93RE3
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant wild-type and mutant enzymes from Escherichia coli
-
recombinant wild-type and mutant enzymes from Escherichia coli strain Bl21(DE3)
-
native enzyme from cell extract 86fold to homogeneity by several chromatographic steps
-
ammonium sulfate precipitation, Matrex Red A column chromatography, DEAE-5PW column chromatography, hydroxyapatite column chromatography, and Superdex-200 gel filtration
-
recombinant His-tagged mtFNR to homogeneity from Escherichia coli by nickel affinity chromatography
-, Q5CVU8
butyl Toyopearl column chromatography and DEAE Sepharose column chromatography
P28861
soluble enzyme by ultracentrifugation, DEAE ion exchange chromatography, dialysis, and hydroxyapatite chromatography
-
expressed in Escherichia coli
-
Ni-NTA affinity chromatography
-, Q8EY89
soluble recombinant enzyme from Escherichia coli strain BL21(DE3) to homogeneity by ammonium sulfate fractionation, gel filtration, and anion-exchange chromatography
-
phenyl-Superose column chromatography
-
Q-Sepharose Fast Flow column chromatography and Sephadex G-50 gel filtration
-
ultrafiltration and Sephadex G-50 gel filtration
-
DEAE-Sepharose column chromatography and Sephacryl S-300 gel filtration
-
recombinant enzyme from Escherichia coli to homogeneity, native enzyme about 400fold to homogeneity
Q9L6V3
from spinach leaves in several steps, to homogeneity
-
purification method development for cytochrome b6f -associated ferredoxin:NADP+ oxidoreductase, overview
-
recombinant chimeric enzyme, comprising the root NADP-binding domain and the leaf FAD-binding domain, from Escherichia coli
-
34 kDa enzyme form, 78 kDa complexed enzyme by cation exchange chromatography, and gel filtration, active 45 kDa enzyme form to homogeneity by ammonium sulfate precipitation, DEAE ion exchange chromatography, and gel filtration
Q93RE3
preparation of phycobilisomes by sucrose density gradient centrifugation
-
ammonium sulfate precipitation, gel filtration, the TSK column chromatography, and MonoQ column chromatography; ammonium sulfate precipitation. gel filtration, the TSK column chromatography, and MonoQ column chromatography
Q8RVZ8, Q8RVZ9
recombinant wild-type and mutant ferredoxin and Fd-NADP+ reductases from Escherichia coli strain BL21(DE3) the latter as homodimers, separation to monomers and crosslinking, further purification of crosslinked complexes by anion exchange chromatography and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expressed via plasmid in Escherichia coli
P21890
expression of wild-type and mutant enzymes
-
expression of wild-type and mutant enzymes in Escherichia coli strain 0225 and BL21(DE3)
-
expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
-
-, Q9M4D2
expression in Escherichia coli, no posttranslational modification of the recombinant enzyme, the recombinant enzyme shows 26% of native enzyme activity
-
expressed in Escherichia coli Tuner(DE3)pLacI cells
-
mtFNR, sequence comparison and phylogenetic analysis, real-time quantitative RT-PCR expression ananlysis, recombinant expression of the His-tagged enzyme in Escherichia coli strain Rosetta (DE3)
-, Q5CVU8
expressed in Escherichia coli JM109 cells
P28861
expressed in Escherichia coli as recombinant protein
-
expressed in Escherichia coli
-, Q8EY89
gene fprA, expression of the soluble enzyme in Escherichia coli strain BL21(DE3)
-
expression in Nicotiana tabacum
-
; expressed in Escherichia coli
-
expressed in Escherichia coli
-
overexpressed in Escherichia coli
-
expressed in Escherichia coli ArcticExpress RIL cells
-
expressed in Pichia pastoris
-
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed via plasmid in Escherichia coli strain BL21(DE3)
-
gene fpr, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli
Q9L6V3
functional expression of chimeric enzyme, comprising the root NADP-binding domain and the leaf FAD-binding domain, in Escherichia coli
-
two forms, one lacks the first 28 amino acid residues, has full diaphorase activity but reduced NADPH/cytochrome-c activity
-
expression in Escherichia coli
Q96YN9, -
gene petH, DNA and amino acid sequence determination and analysis
Q93RE3
expression of N-terminally truncated gene petH
-
overexpressed as recombinant protein in Escherichia coli
-
recombinant protein
-
co-expression of wild-type and mutant ferredoxin and Fd-NADP+ reductases in Escherichia coli strain BL21(DE3)
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the level of Fpr is significantly increased in Escherichia coli cultured in lower iron concentrations (0.017-12.2 ppm)
P28861
low CO2 enhances the expression and activity of FNR and the cyclic photosystem I mediated by FNR
-
low CO2 enhances the expression and activity of FNR and the cyclic photosystem I mediated by FNR
Synechocystis sp. 6803
-
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E139?
-
different conformation
E139D
-
site-directed mutagenesis, altered conformation compared to the wild-type enzyme, slightly reduced activity compared to the wild-type enzyme
E139K
-
site-directed mutagenesis, mutant enzyme shows increased interaction with ferredoxin and reduces the appropriate orientation of flavodoxin, altered conformation compared to the wild-type enzyme, increased activity compared to the wild-type enzyme
E139K
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
E139Q
-
site-directed mutagenesis, mutant enzyme shows increased interaction with ferredoxin and reduces the appropriate orientation of flavodoxin, altered conformation compared to the wild-type enzyme, increased activity compared to the wild-type enzyme
E301A
-
no significant differences to wild type enzyme
E301A
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
E301A
-
8% FAD semiquinone at the equilibrium. Mutation does not change quinone substrate specificity but confers the mixed single- and two-electron mechanism of quinone reduction, whereas wild-type uses a single-electron pathway. Change can be explained by the relative increase in the rate of second electron transfer
E301A
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
I59A
-
kcat for flavodoxin is slightly decreased, but kcat/Km is markedly increased
I59A/I92A
-
kcat and kcat/Km for flavodoxin are markedly reduced
I59E
-
kcat for flavodoxin is increased, kcat/Km is markedly increased
I59E/I92E
-
kcat and kcat/Km for flavodoxin are markedly reduced
I92A
-
kcat for flavodoxin is increased, kcat/Km is markedly increased
I92E
-
kcat for flavodoxin is increased, kcat/Km is markedly increased
K138E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K290E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K294E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K72E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K75E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
K75E
-
mutation results in changes of charge distribution on the surface of the protein and in formation of a salt bridge between E75 and K72 that inhibits the essential interaction of these residues with flavodoxin/ferredoxin
L263A
-
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
L263P
-
site-directed mutagenesis, altered cofactor specificity compared to the wild-type enzyme
L76D
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L76F
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L76S
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L76V
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78D
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78F
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
L78S
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
R100A
-
amino acid replacement removes the positive charge and the ability to form hydrogen bonds, enzyme interacts weakly with Cibacron-Blue Sepharose, increased Km for NADPH
R100A
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
R100A
-
site-directed mutagensis, kinetic parameters for hydride and deuteride transfer processes between enzyme and NADP+ in comparison to the wild-type enzyme, overview
R16E
-
site-directed mutagenesis, altered interaction and kinetics of enzyme-ferredoxin association compared to the wild-type enzyme
R224Q/R233L/Y235F