| pubmed-article:1846288 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0013846 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0521451 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0010749 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0439857 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:1846288 | lifeskim:mentions | umls-concept:C0086486 | lld:lifeskim |
| pubmed-article:1846288 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:1846288 | pubmed:dateCreated | 1991-2-26 | lld:pubmed |
| pubmed-article:1846288 | pubmed:abstractText | The effect of ionic strength on the one-electron reduction of oxidized bovine cytochrome c oxidase by reduced bovine cytochrome c has been studied by using flavin semiquinone reductants generated in situ by laser flash photolysis. In the absence of cytochrome c, direct reduction of the heme a prosthetic group of the oxidase by the one-electron reductant 5-deazariboflavin semiquinone occurred slowly, despite a driving force of approximately +1 V. This is consistent with a sterically inaccessible heme a center. This reduction process was independent of ionic strength from 10 to 100 mM. Addition of cytochrome c resulted in a marked increase in the amount of reduced oxidase generated per laser flash. Reduction of the oxidase at the heme a site was monophasic, whereas oxidation of cytochrome c was multiphasic, the fastest phase corresponding in rate constant to the reduction of the heme a. During the fast kinetic phase, 2 equiv of cytochrome c was oxidized per heme a reduced. We presume that the second equivalent was used to reduce the Cua center, although this was not directly measured. The first-order rate-limiting process which controls electron transfer to the heme a showed a marked ionic strength effect, with a maximum rate constant occurring at mu = 110 mM (1470 s-1), whereas the rate constant obtained at mu = 10 mM was 630 s-1 and at mu = 510 mM was 45 s-1. There was no effect of "pulsing" the enzyme on this rate-limiting one-electron transfer process. These results suggest that there are structural differences in the complex(es) formed between mitochondrial cytochrome c and cytochrome c oxidase at very low and more physiologically relevant ionic strengths, which lead to differences in electron-transfer rate constants. | lld:pubmed |
| pubmed-article:1846288 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1846288 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1846288 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1846288 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1846288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1846288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1846288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1846288 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1846288 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1846288 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:1846288 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:1846288 | pubmed:author | pubmed-author:TollinGG | lld:pubmed |
| pubmed-article:1846288 | pubmed:author | pubmed-author:HazzardJ TJT | lld:pubmed |
| pubmed-article:1846288 | pubmed:author | pubmed-author:RongS YSY | lld:pubmed |
| pubmed-article:1846288 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1846288 | pubmed:day | 8 | lld:pubmed |
| pubmed-article:1846288 | pubmed:volume | 30 | lld:pubmed |
| pubmed-article:1846288 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1846288 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1846288 | pubmed:pagination | 213-22 | lld:pubmed |
| pubmed-article:1846288 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
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| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
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| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
| pubmed-article:1846288 | pubmed:meshHeading | pubmed-meshheading:1846288-... | lld:pubmed |
| pubmed-article:1846288 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1846288 | pubmed:articleTitle | Ionic strength dependence of the kinetics of electron transfer from bovine mitochondrial cytochrome c to bovine cytochrome c oxidase. | lld:pubmed |
| pubmed-article:1846288 | pubmed:affiliation | Department of Biochemistry, University of Arizona, Tucson 85721. | lld:pubmed |
| pubmed-article:1846288 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1846288 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1846288 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1846288 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1846288 | lld:pubmed |
