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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.
i.e. AlkG. Isoform RubB can reduce AlkG, therefore compensating for the absence of AlkT, also a rubredoxin reductase, missing inAlcanivorax borkumensis SK2 genome
i.e. AlkG. Isoform RubB can reduce AlkG, therefore compensating for the absence of AlkT, also a rubredoxin reductase, missing inAlcanivorax borkumensis SK2 genome
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
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
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
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
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
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
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
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
enzyme interacts with its physiological partner NADH:flavorubredoxin oxidoreductase. Redox properties and mechanism of electron transfer are fine-tuned upon the interaction
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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
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
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
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
Solution structure of the two-iron rubredoxin of Pseudomonas oleovorans determined by NMR spectroscopy and solution X-ray scattering and interactions with rubredoxin reductase
Redox and spectroscopic properties of the Escherichia coli nitric oxide-detoxifying system involving flavorubredoxin and its NADH-oxidizing redox partner
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