Source:http://linkedlifedata.com/resource/pubmed/id/11440857
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
7
|
| pubmed:dateCreated |
2001-7-6
|
| pubmed:abstractText |
Recently, crystallographic, spectroscopic, kinetic and biochemical genetic data have merged to unveil a large domain movement for the Fe-S subunit in cytochrome bc(1). In this evolutionarily conserved enzyme, the domain motion acts to conduct intra-complex electron transfer and is essential for redox energy conversion.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Jul
|
| pubmed:issn |
0968-0004
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
26
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
445-51
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:11440857-Catalysis,
pubmed-meshheading:11440857-Electron Transport,
pubmed-meshheading:11440857-Electron Transport Complex III,
pubmed-meshheading:11440857-Models, Chemical,
pubmed-meshheading:11440857-Models, Molecular,
pubmed-meshheading:11440857-Oxygen,
pubmed-meshheading:11440857-Protein Structure, Tertiary,
pubmed-meshheading:11440857-Proteins,
pubmed-meshheading:11440857-Thermodynamics
|
| pubmed:year |
2001
|
| pubmed:articleTitle |
Large scale domain movement in cytochrome bc(1): a new device for electron transfer in proteins.
|
| pubmed:affiliation |
Service de Biochimie Post-génomique et Toxicologie Nucléaire, DIEP, DSV, CEA VALRHO, 30207, Bagnols sur Cèze, France.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review
|