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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3-4
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pubmed:dateCreated |
1985-8-28
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pubmed:abstractText |
When pulsed cytochrome c oxidase is exposed to carbon monoxide in the absence of oxygen the enzyme is converted quickly to its CO-associated mixed valence state. The half-time for this reaction at 0 degree C is about 4 min. This is about 100 times faster than a similar reaction which begins with the resting form of the enzyme. The possible significance of this reaction in understanding the pulsed/resting phenomenon and the carbon monoxide oxygenase reactions of cytochrome oxidase is discussed.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0162-0134
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
23
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
295-302
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:2991470-Animals,
pubmed-meshheading:2991470-Carbon Monoxide,
pubmed-meshheading:2991470-Cattle,
pubmed-meshheading:2991470-Electron Transport Complex IV,
pubmed-meshheading:2991470-Enzyme Activation,
pubmed-meshheading:2991470-Kinetics,
pubmed-meshheading:2991470-Myocardium,
pubmed-meshheading:2991470-Oxidation-Reduction,
pubmed-meshheading:2991470-Spectrophotometry
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pubmed:articleTitle |
The reactivity of pulsed cytochrome c oxidase toward carbon monoxide.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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