Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
17
|
pubmed:dateCreated |
1990-1-5
|
pubmed:abstractText |
Intramolecular electron transfer in partially reduced cytochrome c oxidase has been studied by the perturbed equilibrium method. We have prepared a three-electron-reduced, CO-inhibited form of the enzyme in which cytochrome a and copper A are partially reduced and in an intramolecular redox equilibrium. When these samples were irradiated with a nitrogen laser (0.6-ns, 1.0-mJ pulses) to photodissociate the bound CO, changes in absorbance at 598 and 830 nm were observed which were consistent with a fast electron transfer from cytochrome a to copper A. The absorbance changes at 598 nm gave an apparent rate of 17,000 +/- 2000 s-1 (1 sigma), at pH 7.0 and 25.5 degrees C. These changes were not observed in either the CO mixed-valence or the CO-inhibited fully reduced forms of the enzyme. The rate was fastest at about pH 8.0, falling off toward both lower and higher pHs. There was a small but clear temperature dependence. The process was also observed in the cytochrome c-cytochrome c oxidase high-affinity complex. The electron equilibration measured between cytochrome a and copper A is far faster than any rate measured or inferred previously for this process.
|
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 |
22
|
pubmed:volume |
28
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
6975-83
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:2554962-Animals,
pubmed-meshheading:2554962-Copper,
pubmed-meshheading:2554962-Cytochrome a Group,
pubmed-meshheading:2554962-Cytochromes,
pubmed-meshheading:2554962-Electron Transport,
pubmed-meshheading:2554962-Electron Transport Complex IV,
pubmed-meshheading:2554962-Horses,
pubmed-meshheading:2554962-Kinetics,
pubmed-meshheading:2554962-Mitochondria, Heart,
pubmed-meshheading:2554962-Oxidation-Reduction,
pubmed-meshheading:2554962-Spectrophotometry,
pubmed-meshheading:2554962-Time Factors
|
pubmed:year |
1989
|
pubmed:articleTitle |
Electron transfer between cytochrome a and copper A in cytochrome c oxidase: a perturbed equilibrium study.
|
pubmed:affiliation |
Arthur Amos Noyes Laboratory of Chemical Physics, California Institute of Technology, Pasadena 91125.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
|