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Information on EC 1.3.7.7 - ferredoxin:protochlorophyllide reductase (ATP-dependent) and Organism(s) Prochlorococcus marinus and UniProt Accession Q7VD39

for references in articles please use BRENDA:EC1.3.7.7
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EC Tree
IUBMB Comments
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
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Prochlorococcus marinus
UNIPROT: Q7VD39
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Word Map
The taxonomic range for the selected organisms is: Prochlorococcus marinus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
light-independent protochlorophyllide reductase, dark protochlorophyllide reductase, light-independent pchlide reductase, dark-operative pchlide oxidoreductase, light-independent (dark-operative) pchlide oxidoreductase, dark-operative protochlorophyllide reductase, protochlorophyllide oxidoreductase complex, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dark-operative protochlorophyllide oxidoreductase
-
protochlorophyllide oxidoreductase complex
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dark operative protochlorophyllide oxidoreductase
-
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dark-operative Pchlide oxidoreductase
-
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protochlorophyllide oxidoreductase
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
show the reaction diagram
dynamic switch mechanism of DPOR, catalytic mechanism and structure-function analysis, detailed overview
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate = protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
show the reaction diagram
reaction mechanism and structure-function relationship, overview
-
SYSTEMATIC NAME
IUBMB Comments
ATP-dependent ferredoxin:protochlorophyllide-a 7,8-oxidoreductase
Occurs in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms. The enzyme catalyses trans-reduction of the D-ring of protochlorophyllide; the product has the (7S,8S)-configuration. Unlike EC 1.3.1.33 (protochlorophyllide reductase), light is not required. The enzyme contains a [4Fe-4S] cluster, and structurally resembles the Fe protein/MoFe protein complex of nitrogenase (EC 1.18.6.1), which catalyses an ATP-driven reduction.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
additional information
?
-
-
proposed catalytic redox cycle of DPOR, overview
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
?
protochlorophyllide a + reduced ferredoxin + 2 ATP + 2 H2O
chlorophyllide a + oxidized ferredoxin + 2 ADP + 2 phosphate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
proposed catalytic redox cycle of DPOR, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
two redox-active [4Fe-4S] clusters, both [4Fe-4S] clusters are centered around the extended axis: the L2 cluster is symmetrically ligated by four cysteinyl ligands between the two subunits, whereas the NB cluster is asymmetrically ligated by three cysteine residues from subunit N and one aspartate residue from subunit B
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
protein-protein interaction surfaces for transition state complexes of DPOR and nitrogenase, using PDB ID code 1M34, analysis of catalytic differences and similarities between DPOR and nitrogenase, overview
physiological function
during chlorophyll biosynthesis in photosynthetic bacteria, cyanobacteria, green algae and gymnosperms, dark-operative protochlorophyllide oxidoreductase, a nitrogenase-like metalloenzyme, catalyzes the chemically challenging two-electron reduction of the fully conjugated ring system of protochlorophyllide a. The reduction of the C-17=C-18 double bond results in the characteristic ring architecture of all chlorophylls, thereby altering the absorption properties of the molecule and providing the basis for light-capturing and energytransduction processes of photosynthesis
evolution
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
360000
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enzyme complex, gel filtration
45000
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octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
46199
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
58729
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octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
60000
-
octameric (ChlN/ChlB)2(ChlL2)2 subunit complex, 4 * 35000, subunit ChlL, + 2 * 45000, subunit ChlN, 2 * 60000, subunit ChlB, SDS-PAGE, 4 * 32395,subunit ChlL, + 2 * 46199, subunit ChlN, 2 * 58729, subunit ChlB, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
octamer
(L2)2(NB)2 enzyme complex with perfect symmetry. Subunits L2 and NifH2 both contain a subunit-bridging [4Fe-4S] cluster, whereas the [4Fe-4S] cluster at the N/B subunit interface of (NB)2 is located in an analogous position as the [8Fe-7S] P-cluster at the NifD/NifK subunit interface of (NifDK)2
octamer
additional information
-
DPOR consists of two components: a reductase component designated L-protein (a BchL dimer) and a catalytic component named NB-protein (a BchN-BchB heterotetramer), structure analysis and comparison to the nitrogenase complex, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
substrate-bound, ADP-aluminium fluoride-stabilized transition state complex between the DPOR components L2 and (NB)2, sitting drops by vapor diffusion, mixing of 0.001 ml of protein solution containing 7.5 mg/ml protein in 100 mM HEPES/NaOH, pH 7.5, 150 mM NaCl, 10 mM MgCl2, 50 mM NaF, and 2 mM AlCl3,with 0.001 ml of reservoir solution containing 0.1 M KCl, 0.1 M Tris, pH 8.5, and 3% wt/v PEG 6000, 17°C, X-ray diffraction structure determination and analysis at 2.1 A resolution
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the ternary DPOR enzyme holocomplex comprising subunits ChlN, ChlB, and ChlL is trapped as an octameric (ChlN/ChlB)2(ChlL2)2 complex after incubation with the nonhydrolyzable ATP analogues adenosine 5'-(gamma-thio)triphosphate, adenosine 5'-(beta,gamma-imido)triphosphate, or MgADP in combination with AlF4-, complex structure, overview. A mutant ChlL2 protein, with a deleted Leu153 in the switch II region also allows for the formation of a stable octameric complex
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification by immobilization of GST-tagged subunit L2 on glutathione resin, complex formation with purified subunits NB, and proteolytical cleavage
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Broecker, M.J.; Waetzlich, D.; Saggu, M.; Lendzian, F.; Moser, J.; Jahn, D.
Biosynthesis of (bacterio)chlorophylls: ATP-dependent transient subunit interaction and electron transfer of dark operative protochlorophyllide oxidoreductase
J. Biol. Chem.
285
8268-8277
2010
Prochlorococcus marinus
Manually annotated by BRENDA team
Moser, J.; Broecker, M.J.
Methods for nitrogenase-like dark operative protochlorophyllide oxidoreductase
Methods Mol. Biol.
766
129-143
2011
Prochlorococcus marinus
Manually annotated by BRENDA team
Moser, J.; Lange, C.; Krausze, J.; Rebelein, J.; Schubert, W.D.; Ribbe, M.W.; Heinz, D.W.; Jahn, D.
Structure of ADP-aluminium fluoride-stabilized protochlorophyllide oxidoreductase complex
Proc. Natl. Acad. Sci. USA
110
2094-2098
2013
Prochlorococcus marinus (Q7VD39), Prochlorococcus marinus
Manually annotated by BRENDA team
Reinbothe, C.; El Bakkouri, M.; Buhr, F.; Muraki, N.; Nomata, J.; Kurisu, G.; Fujita, Y.; Reinbothe, S.
Chlorophyll biosynthesis: spotlight on protochlorophyllide reduction
Trends Plant Sci.
15
614-624
2010
Cereibacter sphaeroides, Chlorobaculum tepidum, Chloroflexus aurantiacus, Heliobacterium mobile, Prochlorococcus marinus, Rhodobacter capsulatus
Manually annotated by BRENDA team