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PrrC, a Sco homologue from Rhodobacter sphaeroides , possesses thiol‐disulfide oxidoreductase activity
Author(s) -
Badrick Alison C.,
Hamilton Amanda J.,
Bernhardt Paul V.,
Jones Christopher E.,
Kappler Ulrike,
Jennings Michael P.,
McEwan Alastair G.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.08.058
Subject(s) - rhodobacter sphaeroides , oxidoreductase , thiol , chemistry , disulfide bond , biochemistry , stereochemistry , rhodospirillales , enzyme , photosynthesis
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.