| pubmed-article:8395206 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8395206 | lifeskim:mentions | umls-concept:C0013846 | lld:lifeskim |
| pubmed-article:8395206 | lifeskim:mentions | umls-concept:C0010760 | lld:lifeskim |
| pubmed-article:8395206 | lifeskim:mentions | umls-concept:C0243072 | lld:lifeskim |
| pubmed-article:8395206 | pubmed:issue | 33 | lld:pubmed |
| pubmed-article:8395206 | pubmed:dateCreated | 1993-9-27 | lld:pubmed |
| pubmed-article:8395206 | pubmed:abstractText | The reactions of bovine cytochrome c oxidase with horse cytochrome c derivatives labeled at specific lysine amino groups with (dicarboxybipyridine)bis(bipyridine)ruthenium (II) were studied by laser flash photolysis. All of the derivatives form complexes with cytochrome c oxidase at low ionic strength (5 mM sodium phosphate, pH 7). Excitation of Ru(II) to Ru(II*) with a short laser flash resulted in rapid electron transfer to the ferric heme group of cytochrome c, followed by electron transfer to cytochrome c oxidase. The photoreduced heme Fe(II) in the cytochrome c derivative modified at lysine 25 on the periphery of the heme crevice domain transferred an electron to CuA with a rate constant of 1.1 x 10(4) s-1. CuA then transferred an electron to cytochrome a with a rate constant of 2.3 x 10(4) s-1. The derivatives modified at lysines 7, 39, 55, and 60 remote from the heme crevice domain of cytochrome c have nearly the same kinetics. The rate constant for electron transfer from the cytochrome c heme to CuA is greater than 10(5) s-1, and the rate constant for electron transfer from CuA to cytochrome a is 2 x 10(4) s-1. The cytochrome c derivatives modified at lysines 13 and 27 in the heme crevice domain react much more slowly than the other derivatives, with intracomplex rate constants for oxidation of cytochrome c ranging from 1000 to 6000 s-1. The bulky ruthenium group at the heme crevice domain of these derivatives apparently alters the binding orientation, leading to smaller electron-transfer rates.(ABSTRACT TRUNCATED AT 250 WORDS) | lld:pubmed |
| pubmed-article:8395206 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8395206 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8395206 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8395206 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8395206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8395206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8395206 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8395206 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8395206 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8395206 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8395206 | pubmed:author | pubmed-author:HaiD MDM | lld:pubmed |
| pubmed-article:8395206 | pubmed:author | pubmed-author:MillettFF | lld:pubmed |
| pubmed-article:8395206 | pubmed:author | pubmed-author:LAWR GRG | lld:pubmed |
| pubmed-article:8395206 | pubmed:author | pubmed-author:DurhamBB | lld:pubmed |
| pubmed-article:8395206 | pubmed:author | pubmed-author:HibdonSS | lld:pubmed |
| pubmed-article:8395206 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8395206 | pubmed:day | 24 | lld:pubmed |
| pubmed-article:8395206 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8395206 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8395206 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8395206 | pubmed:pagination | 8492-8 | lld:pubmed |
| pubmed-article:8395206 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:meshHeading | pubmed-meshheading:8395206-... | lld:pubmed |
| pubmed-article:8395206 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8395206 | pubmed:articleTitle | Intracomplex electron transfer between ruthenium-cytochrome c derivatives and cytochrome c oxidase. | lld:pubmed |
| pubmed-article:8395206 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville 72701. | lld:pubmed |
| pubmed-article:8395206 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8395206 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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