Linked Life Data

9261111

Source:http://linkedlifedata.com/resource/pubmed/id/9261111

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
34
pubmed:dateCreated
1997-9-15
pubmed:abstractText
ArsC encoded by Escherichia coli plasmid R773 catalyzes the reduction of arsenate to arsenite. The enzymatic reaction requires reduced glutathione and glutaredoxin. In this study a direct association between ArsC and glutaredoxin was demonstrated. An arsC gene with six histidine codons added to the 5' end of the gene was constructed, and the resulting ArsC enyzme was shown to be functional. Interaction of the histidine-tagged ArsC and glutaredoxin was examined by Ni2+ affinity chromatography. The association required the presence of reduced glutathione and either the substrate arsenate or a competitive inhibitor, phosphate or sulfate. A free thiolate on glutathione was not required. A tryptophan residue was introduced into ArsC at the 11th position, immediately adjacent to the active site Cys-12. Trp-11 fluorescence was quenched upon addition of arsenate. Addition of reduced glutathione after arsenate resulted in a rapid increase in fluorescence followed by a slower decay of the signal. These spectroscopic signals were specific for arsenate and reduced glutathione; neither competitive inhibitors nor non-thiol glutathione analogs produced this effect. Cys-12 thiolate was also required. Thus the intrinsic fluorescence of Trp-11 provides a useful probe to investigate the mechanism of this novel reductase.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
21084-9
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Ligand interactions of the ArsC arsenate reductase.
pubmed:affiliation
Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.