Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.18.1.1 extracted from

  • 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 (2010), Proteins, 78, 1066-1070.
    View publication on PubMed

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, structure modelling, overview Clostridium acetobutylicum

Organism

Organism UniProt Comment Textmining
Clostridium acetobutylicum Q9AL95
-
-

Subunits

Subunits Comment Organism
monomer NROR exists as a monomer in solution, the overall structure of NROR displays a GR-fold Clostridium acetobutylicum

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
FAD binding structure, overview Clostridium acetobutylicum
NADH binding structure, overview Clostridium acetobutylicum

General Information

General Information Comment Organism
additional information the enzyme's disulfide bonds are not involved in the electron transfer from NADH to rubredoxin catalyzed by NROR Clostridium acetobutylicum