Linked Life Data

3030819

Source:http://linkedlifedata.com/resource/pubmed/id/3030819

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-5-4
pubmed:abstractText
The resting as well as the 420 nm and 428 nm forms of cytochrome oxidase have been studied in kinetic experiments with an excess of enzyme over reduced cytochrome c. No difference was found in the behavior of the two activated forms. With all three forms, a fraction of cytochrome a was reoxidized with a rate which was much lower than kcat. This suggests that intramolecular transfer to the dioxygen-reducing site occurs only if both cytochrome a and CuA are reduced. An initial rapid phase in the oxidation of cytochrome a in the pulsed and oxygenated enzymes is related to the presence of a three-electron-reduced dioxygen intermediate. The increased catalytic activity of pulsed and oxygenated oxidase can be explained on the basis of a shift in the redox equilibrium between cytochrome a and CuA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
23
pubmed:volume
213
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
396-400
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Two-electron reduction is required for rapid internal electron transfer in resting, pulsed and oxygenated cytochrome c oxidase.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't