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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1975-8-4
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pubmed:abstractText |
1. Upon addition of sulphide to oxidized cytochrome c oxidase, a low-spin heme sulphide compound is formed with an EPR signal at gx = 2.54, gy = 2.23 and gz = 1.87. Concomitantly with the formation of this signal the EPR-detectable low-spin heme signal at g = 3 and the copper signal near g = 2 decrease in intensity, pointing to a partial reduction of the enzyme by sulphide. 2. The addition of sulphide to cytochrome c oxidase, previously reduced in the presence of azide or cyanide, brings about a disappearance of the azido-cytochrome c oxidase signal at gx = 2.9, gy = 2.2, and gz = 1.67 and a decrease of the signal at g = 3.6 of cyano-cytochrome c oxidase. Concomitantly the sulphide-induced EPR signal is formed. 3. These observations demonstrate that azide, cyanide and sulphide are competitive for an oxidized binding site on cytochrome c oxidase. Moreover, it is shown that the affinity of cyanide and sulphide for this site is greater than that of azide.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Azides,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Cyanides,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
http://linkedlifedata.com/resource/pubmed/chemical/Heme,
http://linkedlifedata.com/resource/pubmed/chemical/Sulfides
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
387
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
189-93
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pubmed:dateRevised |
2009-11-3
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pubmed:meshHeading |
pubmed-meshheading:164940-Animals,
pubmed-meshheading:164940-Azides,
pubmed-meshheading:164940-Binding Sites,
pubmed-meshheading:164940-Cattle,
pubmed-meshheading:164940-Copper,
pubmed-meshheading:164940-Cyanides,
pubmed-meshheading:164940-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:164940-Electron Transport Complex IV,
pubmed-meshheading:164940-Heme,
pubmed-meshheading:164940-Myocardium,
pubmed-meshheading:164940-Oxidation-Reduction,
pubmed-meshheading:164940-Protein Binding,
pubmed-meshheading:164940-Protein Conformation,
pubmed-meshheading:164940-Sulfides
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pubmed:year |
1975
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pubmed:articleTitle |
Biochemical and biophysical studies on cytochrome c oxidase. XX. Reaction with sulphide.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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