| pubmed-article:8645176 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8645176 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:8645176 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:8645176 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:8645176 | lifeskim:mentions | umls-concept:C0452849 | lld:lifeskim |
| pubmed-article:8645176 | pubmed:dateCreated | 1996-7-15 | lld:pubmed |
| pubmed-article:8645176 | pubmed:abstractText | A covalent complex between cytochrome c oxidase and Saccharomyces cerevisiae iso-1-cytochrome c (called caa3) has been prepared at low ionic strength. Subunit III Cys-115 of beef heart cytochrome c oxidase cross-links by disulphide bond formation to thionitrobenzoate-modified yeast cytochrome c, a derivative shown to bind into the high-affinity site for substrate [Fuller, Darley-Usmar and Capaldi (1981) Biochemistry 20, 7046-7053]. Stopped-flow experiments show that (1) covalently bound yeast cytochrome c cannot donate electrons to cytochrome oxidase, whereas oxidation of exogenously added cytochrome c and electron transfer to cytochrome a are only slightly affected; (2) the steady-state reduction levels of cytochrome c and cytochrome a in the covalent complex caa3 are higher than those found in the native aa3 enzyme. However, (3) K(m) and Vmax values obtained from the non-linear Eadie-Hofstee plots are very similar in both caa3 and aa3. The results imply that cytochrome c bound to the high-affinity site is not in a configuration optimal for electron transfer. | lld:pubmed |
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| pubmed-article:8645176 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8645176 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8645176 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8645176 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8645176 | pubmed:month | May | lld:pubmed |
| pubmed-article:8645176 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:BrunoriMM | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:NicolettiFF | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:SartiPP | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:AntoniniGG | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:MalatestaFF | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:D'ItriEE | lld:pubmed |
| pubmed-article:8645176 | pubmed:author | pubmed-author:GiuffréBB | lld:pubmed |
| pubmed-article:8645176 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8645176 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:8645176 | pubmed:volume | 315 ( Pt 3) | lld:pubmed |
| pubmed-article:8645176 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8645176 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8645176 | pubmed:pagination | 909-16 | lld:pubmed |
| pubmed-article:8645176 | pubmed:dateRevised | 2010-9-13 | lld:pubmed |
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| pubmed-article:8645176 | pubmed:meshHeading | pubmed-meshheading:8645176-... | lld:pubmed |
| pubmed-article:8645176 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8645176 | pubmed:articleTitle | Probing the high-affinity site of beef heart cytochrome c oxidase by cross-linking. | lld:pubmed |
| pubmed-article:8645176 | pubmed:affiliation | Dipartimento di Biologia di Base ed Applicata, Universita' di L'Aquila, Italy. | lld:pubmed |
| pubmed-article:8645176 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8645176 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:8645176 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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