Linked Life Data

20886839

Source:http://linkedlifedata.com/resource/pubmed/id/20886839

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
44
pubmed:dateCreated
2011-4-19
pubmed:databankReference
pubmed:abstractText
Cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774 appears to be capable of receiving two protons and two electrons from hydrogenase for transport to the membrane, and converting electronic energy into proton motive force. Detailed studies of the mechanism require control both of the redox state and of the protonation state of the protein; hence, structure determination of the protein in solution by NMR is the preferred method. This work compares the structures of the protonated protein in the fully oxidized and fully reduced states as a first step toward elucidating the pH-dependent and redox-state-dependent conformational changes that drive the energy transduction. These high-resolution structures revealed significant localized differences upon change of redox state, even though the global folds of the two families of structures are similar. There are concerted redox-linked motions within the protein that bring E61 and K75 closer to heme II in the oxidized form. This is consistent with an electrostatically driven movement that may provide an important contribution to the previously measured positive cooperativity between hemes I and II. No significant conformational changes were observed that might be related to redox?Bohr effects; the families of structures represent mainly protonated forms, and therefore, pH dependence should not play a major role in the observed structural rearrangements.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
9
pubmed:volume
49
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9620-9
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774.
pubmed:affiliation
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't