Linked Life Data

21352493

Source:http://linkedlifedata.com/resource/pubmed/id/21352493

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2011-9-2
pubmed:abstractText
Electron transfer proteins transport electrons safely between large redox enzymes. The complexes formed by these proteins are among the most transient. The biological function requires, on the one hand, sufficient specificity of the interaction to allow for rapid and selective electron transfer, and, on the other hand, a fast turnover of the complex. Recent progress in the characterization of the nature of these complexes has demonstrated that the encounter state plays an important role. This state of initial binding is dominated by electrostatic interactions, and consists of an ensemble of orientations. Paramagnetic relaxation enhancement NMR and chemical shift perturbation analysis provide ways for the experimental characterisation of the encounter state. Several studies that have used these techniques have shown that the surface area sample in the encounter state can be limited to the immediate environment of the final, specific complex. The encounter complex can represent a large fraction and, in some small complexes, no specific binding is detected at all. It can be concluded that, in electron transfer protein complexes, a fine balance is sought between the low-specificity encounter state and the high-specificity productive complex to meet the opposing requirements of rapid electron transfer and a high turnover rate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1742-4658
pubmed:author
pubmed:copyrightInfo
© 2011 The Authors Journal compilation © 2011 FEBS.
pubmed:issnType
Electronic
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1391-400
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Dynamics in electron transfer protein complexes.
pubmed:affiliation
Leiden Institute of Chemistry, Leiden University, Gorlaeus Laboratories, The Netherlands.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't