Source:http://linkedlifedata.com/resource/pubmed/id/15777008
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
71
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pubmed:dateCreated |
2005-3-21
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pubmed:abstractText |
TMADH (trimethylamine dehydrogenase) is a complex iron-sulphur flavoprotein that forms a soluble electron-transfer complex with ETF (electron-transferring flavoprotein). The mechanism of electron transfer between TMADH and ETF has been studied using stopped-flow kinetic and mutagenesis methods, and more recently by X-ray crystallography. Potentiometric methods have also been used to identify key residues involved in the stabilization of the flavin radical semiquinone species in ETF. These studies have demonstrated a key role for 'conformational sampling' in the electron-transfer complex, facilitated by two-site contact of ETF with TMADH. Exploration of three-dimensional space in the complex allows the FAD of ETF to find conformations compatible with enhanced electronic coupling with the 4Fe-4S centre of TMADH. This mechanism of electron transfer provides for a more robust and accessible design principle for interprotein electron transfer compared with simpler models that invoke the collision of redox partners followed by electron transfer. The structure of the TMADH-ETF complex confirms the role of key residues in electron transfer and molecular assembly, originally suggested from detailed kinetic studies in wild-type and mutant complexes, and from molecular modelling.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Electron-Transferring Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavins,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases, N-Demethylating,
http://linkedlifedata.com/resource/pubmed/chemical/trimethylamine dehydrogenase
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pubmed:status |
MEDLINE
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pubmed:issn |
0067-8694
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1-14
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:15777008-Animals,
pubmed-meshheading:15777008-Electron-Transferring Flavoproteins,
pubmed-meshheading:15777008-Electrons,
pubmed-meshheading:15777008-Flavins,
pubmed-meshheading:15777008-Free Radicals,
pubmed-meshheading:15777008-Humans,
pubmed-meshheading:15777008-Models, Chemical,
pubmed-meshheading:15777008-Oxidation-Reduction,
pubmed-meshheading:15777008-Oxidoreductases, N-Demethylating,
pubmed-meshheading:15777008-Protein Structure, Quaternary
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pubmed:year |
2004
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pubmed:articleTitle |
Flavin radicals, conformational sampling and robust design principles in interprotein electron transfer: the trimethylamine dehydrogenase-electron-transferring flavoprotein complex.
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pubmed:affiliation |
Department of Biochemistry, University of Leicester, University Road, Leicester LEI 7RH, UK.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't
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