Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase.

@article{Chen1994PurificationCA,
  title={Purification, characterization and properties of an NADH oxidase from Desulfovibrio vulgaris (Hildenborough) and its coupling to adenylyl phosphosulfate reductase.},
  author={Ling-Ling Chen and Jean Yves Le Gall and Ant{\'o}nio V. Xavier},
  journal={Biochemical and biophysical research communications},
  year={1994},
  volume={203 2},
  pages={
          839-44
        }
}
An NADH oxidase was purified from Desulfovibrio vulgaris. This FMN-containing enzyme reacts with oxygen forming hydrogen peroxide with a specific activity of 0.21 mumoles.min-1.mg-1. The molecular weight of the protein was determined to be 65 kDa on 12.5% SDS/PAGE. It shows very low NADH: rubredoxin oxidoreductase activity specifically towards the rubredoxin from the same organism. However, adenylyl phosphosulfate reductase can be fully reduced by NADH with the purified enzyme, suggesting that… CONTINUE READING

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