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

Badrick, Alison C., Hamilton, Amanda J., Bernhardt, Paul V., Jones, Christopher E., Kappler, Ulrike, Jennings, Michael P. and McEwan, Alastair G. (2007) PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity. FEBS Letters, 581 24: 4663-4667. doi:10.1016/j.febslet.2007.08.058

Author Badrick, Alison C.
Hamilton, Amanda J.
Bernhardt, Paul V.
Jones, Christopher E.
Kappler, Ulrike
Jennings, Michael P.
McEwan, Alastair G.
Title PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity
Formatted title
PrrC, a Sco homologue from Rhodobacter sphaeroides, possesses thiol-disulfide oxidoreductase activity
Journal name FEBS Letters   Check publisher's open access policy
ISSN 0014-5793
Publication date 2007-10-02
Year available 2007
Sub-type Article (original research)
DOI 10.1016/j.febslet.2007.08.058
Volume 581
Issue 24
Start page 4663
End page 4667
Total pages 5
Editor Richard Cogdell
Place of publication Amsterdam, The Netherlands
Publisher Elsevier B.V.
Collection year 2008
Language eng
Subject C1
270101 Analytical Biochemistry
250302 Biological and Medical Chemistry
780103 Chemical sciences
Formatted 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.
Keyword Sco
Cytochrome c oxidase
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Created: Fri, 08 Feb 2008, 17:47:33 EST by Ms Alison Badrick on behalf of School of Chemistry & Molecular Biosciences