Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
15
pubmed:dateCreated
2005-7-18
pubmed:abstractText
The CopC protein from Pseudomonas syringae pathovar tomato is expressed as one of four proteins encoded by the operon CopABCD that is responsible for copper resistance. It is a small soluble molecule (10.5 kDa) with a beta-barrel structure and features two distinct copper binding sites, which are highly specific for Cu(I) (K(D) > or = 10(-)(13)) and Cu(II) (K(D) approximately 10(-)(15)). These dissociation constants were estimated via ligand competition experiments monitored by electronic spectral and fluorescence probes. The chemistries of the two copper sites are interdependent. When the Cu(II) site is empty, the Cu(I) ion is oxidized by air, but when both sites are occupied, the molecule is stable in air. The availability of an unoccupied site of higher affinity induces intermolecular transfer of either Cu(I) or Cu(II) while maintaining free copper ion concentrations in solution at sub-picomolar levels. This intriguing copper chemistry is consistent with the proposed role of CopC as a copper carrier in the oxidizing periplasmic space. These properties would allow it to exchange either Cu(I) or Cu(II) with its putative partners CopA, CopB, and CopD, contrasting with the role of the Cu(I) (only) chaperones found in the reducing cytoplasm.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0020-1669
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
44
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
5203-5
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
CopC protein from Pseudomonas syringae: intermolecular transfer of copper from both the copper(I) and copper(II) sites.
pubmed:affiliation
School of Chemistry, University of Melbourne, Victoria 3010, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't