PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity.
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.
Badrick
Alison C
AC
Centre for Metals in Biology, School of Molecular and Microbial Sciences, The University of Queensland, Brisbane, Queensland 4072, Australia.
Hamilton
Amanda J
AJ
Bernhardt
Paul V
PV
Jones
Christopher E
CE
Kappler
Ulrike
U
Jennings
Michael P
MP
McEwan
Alastair G
AG
D002413:Cations, Divalent / Q000737:chemistry; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D004563:Electrochemistry; D007328:Insulin / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D011485:Protein Binding; D011490:Protein Disulfide Reductase (Glutathione) / Q000235:genetics / Q000378:metabolism*; D012242:Rhodobacter sphaeroides / Q000201:enzymology* / Q000235:genetics; D013053:Spectrophotometry; D013879:Thioredoxins / Q000378:metabolism
D002413:Cations, Divalent; D007328:Insulin; D013879:Thioredoxins; D003300:Copper; D011490:Protein Disulfide Reductase (Glutathione)