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Information on EC 1.18.1.1 - rubredoxin-NAD+ reductase
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1.18.1.1 rubredoxin-NAD+ reductaseIUBMB Comments
Requires FAD. The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin. The reaction does not occur when NADPH is substituted for NADH. Contains iron at the redox centre.
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Word Map
The enzyme appears in viruses and cellular organisms
Reaction Schemes
reduced rubredoxin
+
+
=
oxidized rubredoxin
+
Synonyms
(flavo)rubredoxin reductase, ABO_0162, dihydronicotinamide adenine dinucleotide-rubredoxin reductase, DPNH-rubredoxin reductase, EC 1.6.7.2, FIRd-reductase, NAD(P)H:rubredoxin reductase, NADH-rubredoxin oxidoreductase, NADH-rubredoxin reductase, NADH: rubredoxin oxidoreductase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(flavo)rubredoxin reductase
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ABO_0162
dihydronicotinamide adenine dinucleotide-rubredoxin reductase
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DPNH-rubredoxin reductase
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EC 1.6.7.2
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formerly
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FIRd-reductase
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NADH-rubredoxin oxidoreductase
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NADH-rubredoxin reductase
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NADH: rubredoxin oxidoreductase
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NOR
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reduced nicotinamide adenine dinucleotide-rubredoxin reductase
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reductase, rubredoxin-nicotinamide adenine dinucleotide
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rubB
rubredoxin reductase
rubredoxin-NAD reductase
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rubredoxin reductase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH
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2 reduced rubredoxin + NAD+ + H+ = 2 oxidized rubredoxin + NADH
the electron transfer from NAD(P)H to rubredoxin involves a reductive and an oxidative step with respect to the enzyme
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
MetaCyc
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SYSTEMATIC NAME
IUBMB Comments
rubredoxin:NAD+ oxidoreductase
Requires FAD. The enzyme from Clostridium acetobutylicum reduces rubredoxin, ferricyanide and dichlorophenolindophenol, but not ferredoxin or flavodoxin. The reaction does not occur when NADPH is substituted for NADH. Contains iron at the redox centre.
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CAS REGISTRY NUMBER
COMMENTARY
9032-27-3
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
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weak activity
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?
NADH + 2-methyl-1,4-naphthoquinone
NAD+ + 2-methyl-1,4-naphthoquinol
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-
?
NADH + H+ + oxidized methyl thiazolyl tetrazolium
NAD+ + reduced methyl thiazolyl tetrazolium
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
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weak activity
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-
?
NADH + p-iodonitrotetrazolium
NAD+ + reduced p-iodonitrotetrazolium
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-
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
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-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
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?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
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?
NADH + H+ + oxidized methyl thiazolyl tetrazolium
NAD+ + reduced methyl thiazolyl tetrazolium
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?
NADH + H+ + oxidized methyl thiazolyl tetrazolium
NAD+ + reduced methyl thiazolyl tetrazolium
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?
NADH + H+ + oxidized rubredoxin-2
NAD+ + reduced rubredoxin
i.e. AlkG. Isoform RubB can reduce AlkG, therefore compensating for the absence of AlkT, also a rubredoxin reductase, missing inAlcanivorax borkumensis SK2 genome
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NADH + H+ + oxidized rubredoxin-2
NAD+ + reduced rubredoxin
i.e. AlkG. Isoform RubB can reduce AlkG, therefore compensating for the absence of AlkT, also a rubredoxin reductase, missing inAlcanivorax borkumensis SK2 genome
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NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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the induction of rubredoxin reductase, normally observed at pH 4.3 is stopped immediately after the addition of rifampicin. The enzyme could play a role in some deacidification mechanism in relation to proton transport
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?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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very specific towards Desulfovibrio gigas rubredoxin
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?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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enzyme mediates electron transfer from NADH to Desulfovibrio gigas rubredoxin as well as to E. coli flavorubredoxin
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?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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enzyme catalyzes electron transfer not only to the rubredoxin of Pseudomonas oleovorans but also to the lower molecular weight rubredoxins of the anaerobic bacteria Peptostreptococcus elsdenii, Clostridium pasteurianum and Desulfovibrio gigas
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NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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enzyme is required for fatty acid and alkane hydroxylation
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reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
the enzyme and two rubredoxins form a system indipensable for metabolizing n-alkanes, they constitute an electron transport pathway that shuttles reducing equivalents from carbon metabolism to the membrane-bound alkane hydroxylases AlkB1 and AlkB2
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?
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
rubredoxin-rubredoxin reductase complex formation, only a small number of direct interactions govern mutual recognition of RdxR and Rdx, corroborating the transient nature of the complex, overview, substrate binding structure and mechanism, the enzyme discriminates between two types of rubredoxins, RubA2 and RubA1, overview
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?
additional information
?
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enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
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additional information
?
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enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
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additional information
?
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no activity with spinach ferredoxin, putidaredoxin and adrenodoxin
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additional information
?
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diaphorase activity towards ferricyanide
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additional information
?
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both the nonphysiological 1Fe form of rubredoxin and the physiological 2 Fe form combine with rubredoxin reductase to form functional electron transfer complexes. The reductive half-reaction of the rubredoxin reductase occurs by a simple one-step mechanism in which oxidized enzyme is reduced to an enzyme-NAD+ charge-transfer species
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additional information
?
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enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
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additional information
?
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enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
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additional information
?
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enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
the enzyme and two rubredoxins form a system indipensable for metabolizing n-alkanes, they constitute an electron transport pathway that shuttles reducing equivalents from carbon metabolism to the membrane-bound alkane hydroxylases AlkB1 and AlkB2
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?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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the induction of rubredoxin reductase, normally observed at pH 4.3 is stopped immediately after the addition of rifampicin. The enzyme could play a role in some deacidification mechanism in relation to proton transport
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?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
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enzyme is required for fatty acid and alkane hydroxylation
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?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
the electron transfer between the enzyme and rubredoxin involves a redox active Fe3+, which can be substituted for Ni2+, mechanism, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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NROR is a versatile electron donor for scavengers of O2 and reactive oxygen species
additional information
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the enzyme's disulfide bonds are not involved in the electron transfer from NADH to rubredoxin catalyzed by NROR
Show AA Sequence and Transmembrane Helices (643 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
41000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
RdxR consists of two cofactor-binding domains and a C-terminal domain essential for the specific recognition of Rdx, crystal structure analysis, dimerization restricts access to the NAD(P)H binding pocket and results in a steric clash between the modeled adenine moiety of NAD(P)H and alpha-helix alpha8' of the neighboring molecule, RdxR dimers form at high protein concentrations used during crystallization, rather than being functionally relevant, overview
monomer
additional information
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enzyme interacts with its physiological partner NADH:flavorubredoxin oxidoreductase. Redox properties and mechanism of electron transfer are fine-tuned upon the interaction
monomer
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NROR exists as a monomer in solution, the overall structure of NROR displays a GR-fold
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme, sitting-drop vapour-diffusion method, 20°C, 0.001 l of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.0, is mixed with 0.001 ml of reservoir solution containing 35% v/v PEG 400, 0.1 M Tris-HCl, pH 8.5, and 0.15 M MgCl2, and equilibrated against 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.1 A resolution
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purified recombinant His6-tagged enzyme, sitting-drop vapour-diffusion method, 20°C, 0.001 l of 14 mg/ml protein in 20 mM Tris-HCl, pH 7.0, is mixed with 0.001 ml of reservoir solution containing 35% v/v PEG 400, 0.1 M Tris-HCl, pH 8.5, and 0.15 M MgCl2, and equilibrated against 0.1 ml of reservoir solution, X-ray diffraction structure determination and analysis at 2.1 A resolution, structure modelling, overview
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purified recombinant His-tagged enzyme, free or in complex with substrate rubredoxin, sitting drop vapour diffusion method, 20°C, 8.5 mg/ml protein in 100 mM NaCl, 50 mM Tris-HCl, pH 8.0, FAD, and 5 mM 2-mercaptoethanol, in presence or absence of rubredoxin in a 1.2 molar excess, mixing with an equal volume of reservoir solution containing 5% PEG 1000, 40% PEG 300, 0.1 M Tris-HCl, pH 7.0, mother liquor supplemented with 25% PEG 400 is used for cryoprotection, X-ray diffraction structure determination and analysis at 2.3-2.4 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
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study of truncated versions of enzyme, one consisting only of the rubredoxin molecule, the other of its flavodiiron structural core. analysis of interaction with the physiological partner NADH:flavorubredoxin oxidoreductase
additional information
a mutant of Pseudomonas aeruginosa with an isogenic rdxR transposon insertion is unable to grow on hexadecane
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20% glycerol protects against inactivation, prevents loss of FAD from the intact enzyme
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type enzyme from Escherichia coli by nickel affinity and anion exchange chromatography, and gel filtration
recombinant His6-tagged enzyme from Escherichia coli to homogeneity
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recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
amplification from genomic DNA, overexpression as His6-tagged protein in Escherichia coli strain Tuner (DE3)
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gene rdxR or PA5349, expression of His-tagged wild-type enzyme in Escherichia coli
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Petitdemange, H.; Marczak, R.; Blusson, H.; Gay, R.
Isolation and properties of reduced nicotinamide adenine dinucleotiderubredoxin oxidoreductase of Clostridium acetobutylicum
Biochem. Biophys. Res. Commun.
91
1258-1265
1979
Clostridium acetobutylicum
brenda
Marczak, R.; Ballongue, J.; Petitdemange, H.; Gay, R.
Regulation of the biosynthesis of NADH-rubredoxin oxidoreductase in Clostridium acetobutylicum
Curr. Microbiol.
10
165-168
1984
Clostridium acetobutylicum
-
brenda
Ueda, T.; Lode, E.T.; Coon, M.J.
Enzymatic omega-oxidation. VI. Isolation of homogeneous reduced diphosphopyridine nucleotide-rubredoxin reductase
J. Biol. Chem.
247
2109-2116
1972
Pseudomonas oleovorans
brenda
Ueda, T.; Coon, M.J.
Enzymatic oxidation. VII. Reduced diphosphopyridine nucleotide-rubredoxin reductase: properties and function as an electron carrier in hydroxylation
J. Biol. Chem.
247
5010-5016
1972
Pseudomonas oleovorans
brenda
Le Gall, J.
Partial purification and study of NAD:rubredoxin oxidoreductase from D. gigas
Ann. Inst. Pasteur (Paris)
114
109-115
1968
Desulfovibrio gigas
brenda
Claus, R.; Asperger, O.; Kleber, H.P.
Properties of rubredoxin reductase from the alkane-assimilating bacterium Acinetobacter calcoaceticus
Z. Allg. Mikrobiol.
19
695-704
1979
Acinetobacter calcoaceticus
brenda
Chen, L.; Liu, M.Y.; Legall, J.; Fareleira, P.; Santos, H.; Xavier, A.V.
Purification and characterization of an NADH-rubredoxin oxidoreductase involved in the utilization of oxygen by Desulfovibrio gigas
Eur. J. Biochem.
216
443-448
1993
Desulfovibrio gigas
brenda
Lee, H.J.; Basran, J.; Scrutton, N.S.
Electron transfer from flavin to iron in the Pseudomonas oleovorans rubredoxin reductase-rubredoxin electron transfer complex
Biochemistry
37
15513-15522
1998
Pseudomonas oleovorans
brenda
Gomes, C.M.; Vicente, J.B.; Wasserfallen, A.; Teixeira, M.
Spectroscopic studies and characterization of a novel electron-transfer chain from Escherichia coli involving a flavorubredoxin and its flavoprotein reductase partner
Biochemistry
39
16230-16237
2000
Escherichia coli
brenda
Perry, A.; Tambyrajah, W.; Grossmann, J.G.; Lian, L.Y.; Scrutton, N.S.
Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase
Biochemistry
43
3167-3182
2004
Pseudomonas oleovorans
brenda
Vicente, J.B.; Teixeira, M.
Redox and spectroscopic properties of the Escherichia coli nitric oxide-detoxifying system involving flavorubredoxin and its NADH-oxidizing redox partner
J. Biol. Chem.
280
34599-34608
2005
Escherichia coli
brenda
Hagelueken, G.; Wiehlmann, L.; Adams, T.M.; Kolmar, H.; Heinz, D.W.; Tuemmler, B.; Schubert, W.D.
Crystal structure of the electron transfer complex rubredoxin-rubredoxin reductase of Pseudomonas aeruginosa
Proc. Natl. Acad. Sci. USA
104
12276-12281
2007
Pseudomonas aeruginosa, Pseudomonas aeruginosa (Q9HTK9)
brenda
Nishikawa, K.; Shomura, Y.; Kawasaki, S.; Niimura, Y.; Higuchi, Y.
Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum
Acta Crystallogr. Sect. F
66
23-25
2010
Clostridium acetobutylicum, Clostridium acetobutylicum (Q9AL95)
brenda
Nishikawa, K.; Shomura, Y.; Kawasaki, S.; Niimura, Y.; Higuchi, Y.
Crystal structure of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum: A key component of the dioxygen scavenging system in obligatory anaerobes
Proteins
78
1066-1070
2010
Clostridium acetobutylicum, Clostridium acetobutylicum (Q9AL95)
brenda
Teimoori, A.; Ahmadian, S.; Madadkar-Sobhani, A.; Bambai, B.
Rubredoxin reductase from Alcanivorax borkumensis: expression and characterization
Biotechnol. Prog.
27
1383-1389
2011
Alcanivorax borkumensis, Alcanivorax borkumensis (Q0VTB0), Alcanivorax borkumensis SK2 (Q0VTB0)
brenda
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