Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
33
|
pubmed:dateCreated |
1993-9-27
|
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)
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Aug
|
pubmed:issn |
0006-2960
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
24
|
pubmed:volume |
32
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
8492-8
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:8395206-Animals,
pubmed-meshheading:8395206-Cattle,
pubmed-meshheading:8395206-Cytochrome c Group,
pubmed-meshheading:8395206-Electron Transport,
pubmed-meshheading:8395206-Electron Transport Complex IV,
pubmed-meshheading:8395206-Horses,
pubmed-meshheading:8395206-Kinetics,
pubmed-meshheading:8395206-Photolysis,
pubmed-meshheading:8395206-Ruthenium,
pubmed-meshheading:8395206-Thermodynamics,
pubmed-meshheading:8395206-Time Factors
|
pubmed:year |
1993
|
pubmed:articleTitle |
Intracomplex electron transfer between ruthenium-cytochrome c derivatives and cytochrome c oxidase.
|
pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Arkansas, Fayetteville 72701.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|