Linked Life Data

20959106

Source:http://linkedlifedata.com/resource/pubmed/id/20959106

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2010-10-20
pubmed:abstractText
The interaction of cytochrome c with ubiquinol-cytochrome c oxidoreductase (bc? complex) has been studied for >30 years, yet many aspects remain unclear or controversial. We report the first molecular dynamic simulations of the cyt c-bc? complex interaction. Contrary to the results of crystallographic studies, our results show that there are multiple dynamic hydrogen bonds and salt bridges in the cyt c-c? interface. These include most of the basic cyt c residues previously implicated in chemical modification studies. We suggest that the static nature of x-ray structures can obscure the quantitative significance of electrostatic interactions between highly mobile residues. This provides a clear resolution of the discrepancy between the structural data and functional studies. It also suggests a general need to consider dynamic interactions of charged residues in protein-protein interfaces. In addition, a novel structural change in cyt c is reported, involving residues 21-25, which may be responsible for cyt c destabilization upon binding. We also propose a mechanism of interaction between cyt c? monomers responsible for limiting the binding of cyt c to only one molecule per bc? dimer by altering the affinity of the cytochrome c binding site on the second cyt c? monomer.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1542-0086
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Biophysical Society. Published by Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
20
pubmed:volume
99
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2647-56
pubmed:dateRevised
2011-10-20
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
The binding interface of cytochrome c and cytochrome c? in the bc? complex: rationalizing the role of key residues.
pubmed:affiliation
Center for Biophysics & Computational Biology, University of Illinois at Urbana-Champaign, USA.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural