Linked Life Data

10486145

Source:http://linkedlifedata.com/resource/pubmed/id/10486145

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-11-3
pubmed:abstractText
The copper-containing hemocyanins are a class of oxygen-transport proteins whose structures differ in arthropods and molluscs. Crystal structure analyses and amino acid sequence comparisons show that disulfide bonding is a common feature in both arthropod and mollusc hemocyanins. Reduction of the disulfide bonds of a representative set of arthropod and mollusc hemocyanins results in complete loss of their oxygen-binding capacities. Thus, retention of the disulfide bonds is essential to the functional integrity of the oxygen-binding sites in the subunits of this class of oxygen carriers, despite the very different architectures of the arthropod and mollusc molecules. Depending upon the specific hemocyanin, partial to virtually complete restoration of the oxygen-binding capacity occurs when the disulfide-bond reductant is removed by dialysis. The rate at which the functional, active-site geometry is lost and the extent to which it can be restored varies markedly with hemocyanin type, aggregation state, and experimental conditions. Consequently, a comparison of these differences provides a simple, but powerful, way to probe internal and environmental factors that govern physiologically important structure-function relationships in this entire class of oxygen-transport proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
369
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
261-6
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins.
pubmed:affiliation
Department of Chemistry, University of Richmond, Richmond, Virginia, 23713, USA. rtopham@richmond.edu
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.