Rubredoxin Oxidase, a New Flavo-Hemo-Protein, Is the Site of Oxygen Reduction to Water by the "Strict Anaerobe" Desulfovibrio Gigas

Biochem Biophys Res Commun. 1993 May 28;193(1):100-5. doi: 10.1006/bbrc.1993.1595.

Abstract

A rubredoxin-oxygen oxidoreductase, a homodimer with a molecular weight of 43 kDa per monomer, was found to be a component of an electron transfer chain that couples the reduction of oxygen to water with NADH oxidation. This FAD-containing protein appears to contain a new type of heme group. The electron transfer chain is not inhibited by cyanide and azide. In contrast, CO decreases NADH oxidation rate and also induces release of the prosthetic groups from the native terminal reductase.

Publication types

  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Chromatography, Gel
  • Chromatography, Paper
  • Desulfovibrio / enzymology
  • Desulfovibrio / metabolism*
  • Electron Transport
  • Electrophoresis, Polyacrylamide Gel
  • NAD / metabolism
  • Oxidation-Reduction
  • Oxidoreductases / isolation & purification
  • Oxidoreductases / metabolism*
  • Oxygen / metabolism*
  • Spectrophotometry, Ultraviolet
  • Water / metabolism*

Substances

  • Water
  • NAD
  • Oxidoreductases
  • rubredoxin-oxygen oxidoreductase
  • Oxygen