| pubmed-article:3007206 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3007206 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:3007206 | lifeskim:mentions | umls-concept:C1705165 | lld:lifeskim |
| pubmed-article:3007206 | lifeskim:mentions | umls-concept:C1444748 | lld:lifeskim |
| pubmed-article:3007206 | lifeskim:mentions | umls-concept:C0301630 | lld:lifeskim |
| pubmed-article:3007206 | lifeskim:mentions | umls-concept:C2700061 | lld:lifeskim |
| pubmed-article:3007206 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:3007206 | pubmed:dateCreated | 1986-5-7 | lld:pubmed |
| pubmed-article:3007206 | pubmed:abstractText | The slow increase of a cyanide-induced optical change at 437 nm following rapid cyanide inhibition of cytochrome oxidase has been followed as a function of the number of electrons donated from ferrocytochrome c to cytochrome a and CuA. The initial rate of optical change is a parabolic function of this number. The results have been analyzed in terms of a model where addition of electrons causes a conformational transition allowing rapid cyanide binding. The binding is followed by a slow intramolecular responsible for the optical change. The analysis demonstrates that only molecules with both cytochrome a and CuA reduced can undergo the conformational change, which is suggested to be involved in the proton-pump mechanism of the oxidase. | lld:pubmed |
| pubmed-article:3007206 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3007206 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3007206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3007206 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3007206 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:3007206 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:3007206 | pubmed:author | pubmed-author:MalmströmB... | lld:pubmed |
| pubmed-article:3007206 | pubmed:author | pubmed-author:ScholesC PCP | lld:pubmed |
| pubmed-article:3007206 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3007206 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:3007206 | pubmed:volume | 198 | lld:pubmed |
| pubmed-article:3007206 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3007206 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3007206 | pubmed:pagination | 125-9 | lld:pubmed |
| pubmed-article:3007206 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:meshHeading | pubmed-meshheading:3007206-... | lld:pubmed |
| pubmed-article:3007206 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3007206 | pubmed:articleTitle | Two-electron reduction of cytochrome c oxidase triggers a conformational transition. | lld:pubmed |
| pubmed-article:3007206 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3007206 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:3007206 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3007206 | lld:pubmed |
