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

  • Alison C. Badrick
  • , Amanda J. Hamilton
  • , Paul V. Bernhardt
  • , Christopher E. Jones
  • , Ulrike Kappler
  • , Michael P. Jennings
  • , Alastair G. McEwan
  • University of Queensland

Research output: Contribution to journalArticlepeer-review

27 Citations (Scopus)

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 Cu2+ 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.

Original languageEnglish
Pages (from-to)4663-4667
Number of pages5
JournalFEBS Letters
Volume581
Issue number24
DOIs
Publication statusPublished - 2 Oct 2007
Externally publishedYes

Keywords

  • Copper
  • Cytochrome c oxidase
  • Insulin
  • Sco
  • Thioredoxin

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