PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity

FEBS Lett. 2007 Oct 2;581(24):4663-7. doi: 10.1016/j.febslet.2007.08.058. Epub 2007 Sep 4.

Abstract

PrrC is a Sco homologue in Rhodobacter sphaeroides that is associated with PrrBA, a two-component signal transduction system that induces photosynthesis gene expression in response to a decrease in oxygen tension. Although Sco proteins have been shown to bind copper the observation that they are structurally-related to thioredoxins suggested that they might possess thiol-disulfide oxidoreductase activity. Our results show that PrrC reduces Cu(2+) to Cu(+) and possesses disulfide reductase activity. These results indicate that some bacterial Sco proteins may have biochemical properties that are distinct from those of mitochondrial Sco proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cations, Divalent / chemistry
  • Copper / chemistry
  • Copper / metabolism
  • Electrochemistry
  • Insulin / chemistry
  • Insulin / metabolism
  • Oxidation-Reduction
  • Protein Binding
  • Protein Disulfide Reductase (Glutathione) / genetics
  • Protein Disulfide Reductase (Glutathione) / metabolism*
  • Rhodobacter sphaeroides / enzymology*
  • Rhodobacter sphaeroides / genetics
  • Spectrophotometry
  • Thioredoxins / metabolism

Substances

  • Cations, Divalent
  • Insulin
  • Thioredoxins
  • Copper
  • Protein Disulfide Reductase (Glutathione)