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Literature summary for 1.18.1.1 extracted from

  • Nishikawa, K.; Shomura, Y.; Kawasaki, S.; Niimura, Y.; Higuchi, Y.
    Crystallization and preliminary X-ray analysis of NADH:rubredoxin oxidoreductase from Clostridium acetobutylicum (2010), Acta Crystallogr. Sect. F, 66, 23-25.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
amplification from genomic DNA, overexpression as His6-tagged protein in Escherichia coli strain Tuner (DE3) Clostridium acetobutylicum

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Clostridium acetobutylicum

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum Q9AL95
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant His6-tagged enzyme from Escherichia coli to homogeneity Clostridium acetobutylicum

Synonyms

Synonyms Comment Organism
NADH:rubredoxin oxidoreductase
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Clostridium acetobutylicum
NROR
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Clostridium acetobutylicum

Expression

Organism Comment Expression
Clostridium acetobutylicum NROR is an O2-inducible protein up

General Information

General Information Comment Organism
physiological function NROR is a versatile electron donor for scavengers of O2 and reactive oxygen species Clostridium acetobutylicum