| pubmed-article:6098268 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6098268 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:6098268 | lifeskim:mentions | umls-concept:C0010505 | lld:lifeskim |
| pubmed-article:6098268 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:6098268 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
| pubmed-article:6098268 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:6098268 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:6098268 | pubmed:dateCreated | 1985-3-6 | lld:pubmed |
| pubmed-article:6098268 | pubmed:abstractText | The inhibition of cytochrome c oxidase by cyanide, starting either with the resting or the pulsed enzyme, was studied by rapid-freeze quenching followed by quantitative e.p.r. It is found that a partial reduction of cytochrome oxidase by transfer of 2 electron equivalents from ferrocytochrome c to cytochrome a and CuA will induce a transition from a closed to an open enzyme conformation, rendering the cytochrome a3-CuB site accessible for cyanide binding, possibly as a bridging ligand. A heterogeneity in the enzyme is observed in that an e.p.r. signal from the cytochrome a3 3+-HCN complex is only found in 20% of the molecules, whereas the remaining cyanide-bound a3-CuB sites are e.p.r.-silent. | lld:pubmed |
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| pubmed-article:6098268 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6098268 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6098268 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:6098268 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6098268 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:6098268 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:6098268 | pubmed:author | pubmed-author:WilsonM TMT | lld:pubmed |
| pubmed-article:6098268 | pubmed:author | pubmed-author:JensenPP | lld:pubmed |
| pubmed-article:6098268 | pubmed:author | pubmed-author:MalmströmB... | lld:pubmed |
| pubmed-article:6098268 | pubmed:author | pubmed-author:AasaRR | lld:pubmed |
| pubmed-article:6098268 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6098268 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:6098268 | pubmed:volume | 224 | lld:pubmed |
| pubmed-article:6098268 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6098268 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6098268 | pubmed:pagination | 829-37 | lld:pubmed |
| pubmed-article:6098268 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:6098268 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6098268 | pubmed:articleTitle | Cyanide inhibition of cytochrome c oxidase. A rapid-freeze e.p.r. investigation. | lld:pubmed |
| pubmed-article:6098268 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6098268 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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