Purification and characterization of an NADH oxidase from Eubacterium ramulus.
An NADH oxidase from the strictly anaerobic Eubacterium ramuluswas purified to homogeneity. The enzyme is composed of two types of subunits with molecular masses of 40 and 30 kDa. The molecular mass of the native enzyme is 450 kDa according to gel filtration and PAGE analysis. Six to eight mol of FAD were found per mol of native enzyme. The NADH-specific enzyme was inhibited by N-bromosuccinimide and sulfhydryl reagents such as N-ethylmaleimide, CuCl(2) or ZnCl(2). The physiological function of the purified enzyme is unclear, but the demonstration of NADH-dependent O(2)-consumption suggests that it plays a role in the scavenging of oxygen.
Herles
Claudia
C
Gastrointestinale Mikrobiologie, Deutsches Institut für Ernährungsforschung (DIfE), Arthur-Scheunert-Allee 114-116, 14558 Bergholz-Rehbrücke, Germany.
Braune
Annett
A
Blaut
Michael
M
D000596:Amino Acids / Q000032:analysis; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D005051:Eubacterium / Q000201:enzymology* / Q000302:isolation & purification; D008968:Molecular Conformation; D008970:Molecular Weight; D009097:Multienzyme Complexes / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification*; D009247:NADH, NADPH Oxidoreductases / Q000032:analysis* / Q000737:chemistry / Q000302:isolation & purification*
D000596:Amino Acids; D009097:Multienzyme Complexes; C023107:NADH oxidase; D009247:NADH, NADPH Oxidoreductases