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2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
2 ferricytochrome c + NADH
2 ferrocytochrome c + NAD+ + H+
-
weak activity
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
NADH + 2-methyl-1,4-naphthoquinone
NAD+ + 2-methyl-1,4-naphthoquinol
-
-
-
-
?
NADH + Fe(CN)63-
NAD+ + Fe(CN)64-
-
-
-
-
?
NADH + H+ + 1,4-naphthoquinone
NAD+ + 1,4-naphthoquinol
-
-
-
-
?
NADH + H+ + oxidized methyl thiazolyl tetrazolium
NAD+ + reduced methyl thiazolyl tetrazolium
NADH + H+ + oxidized rubredoxin-2
NAD+ + reduced rubredoxin
NADH + metmyoglobin
NAD+ + reduced metmyoglobin
-
-
-
-
?
NADH + nitroblue tetrazolium
NAD+ + reduced nitroblue tetrazolium
-
weak activity
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
NADH + p-benzoquinone
NAD+ + p-benzoquinol
-
-
-
-
?
NADH + p-iodonitrotetrazolium
NAD+ + reduced p-iodonitrotetrazolium
-
-
-
-
?
NADH + p-toluoquinone
NAD+ + p-toluoquinol
-
-
-
-
?
reduced Desulfovibrio gigas rubredoxin + NAD+ + H+
oxidized Desulfovibrio gigas rubredoxin + NADH
Megalodesulfovibrio gigas
-
-
-
-
r
reduced rubredoxin + NAD(P)+
oxidized rubredoxin + NAD(P)H
reduced rubredoxin + NAD+
oxidized rubredoxin + NADH
-
-
-
-
?
additional information
?
-
2 ferricyanide + NADH

2 ferrocyanide + NAD+ + H+
-
-
-
-
?
2 ferricyanide + NADH
2 ferrocyanide + NAD+ + H+
-
-
-
-
?
NADH + 2,6-dichloroindophenol

NAD+ + reduced 2,6-dichloroindophenol
-
-
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
-
-
-
-
?
NADH + 2,6-dichloroindophenol
NAD+ + reduced 2,6-dichloroindophenol
-
-
-
-
?
NADH + H+ + oxidized methyl thiazolyl tetrazolium

NAD+ + reduced methyl thiazolyl tetrazolium
-
-
-
?
NADH + H+ + oxidized methyl thiazolyl tetrazolium
NAD+ + reduced methyl thiazolyl tetrazolium
-
-
-
?
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
-
-
?
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
-
-
?
NADH + oxidized rubredoxin

NAD+ + reduced rubredoxin
-
-
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
-
-
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
-
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
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
-
enzyme mediates electron transfer from NADH to Desulfovibrio gigas rubredoxin as well as to E. coli flavorubredoxin
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
Megalodesulfovibrio gigas
-
-
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
Megalodesulfovibrio gigas
-
very specific towards Desulfovibrio gigas rubredoxin
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
-
-
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
-
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
-
-
?
NADH + oxidized rubredoxin
NAD+ + reduced rubredoxin
-
enzyme is required for fatty acid and alkane hydroxylation
-
-
?
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
-
-
?
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
-
-
?
additional information

?
-
-
enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
-
enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
-
-
?
additional information
?
-
-
no activity with spinach ferredoxin, putidaredoxin and adrenodoxin
-
-
?
additional information
?
-
-
diaphorase activity towards ferricyanide
-
-
?
additional information
?
-
-
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
-
-
?
additional information
?
-
-
enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
-
-
?
additional information
?
-
-
enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
-
-
?
additional information
?
-
-
enzyme catalyzes rubredoxin-dependent reduction of cytochrome c in presence of NADH
-
-
?
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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
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
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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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
Megalodesulfovibrio 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
Megalodesulfovibrio 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 characteriza