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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
42
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pubmed:dateCreated |
1995-12-14
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pubmed:abstractText |
Upon reaction of cytochrome oxidase with hydrogen peroxide, the spectral changes are complete, with slightly less than 1 equiv of hydrogen peroxide per cytochrome oxidase. At pH 8 the product is a mixture of the P and F forms, while at pH 6 the product is exclusively the F form. These data are inconsistent with current interpretations of the structure of compounds P and F. Two stable radical species are detected by EPR; the relative amounts of these species are pH dependent. The MCD spectra of pure P and F are reported. It is suggested that compound F is a hydrogen peroxide adduct of cytochrome oxidase with cytochrome a3 in the low-spin state and that compound P is an oxyferryl state of cytochrome alpha 3 in support of the recent Raman data of Proshlyakov et al. [(1994) J. Biol. Chem. 269, 29385-29388]. We also suggest that copper B is in the trivalent state in compound P.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Carbon Monoxide,
http://linkedlifedata.com/resource/pubmed/chemical/Copper,
http://linkedlifedata.com/resource/pubmed/chemical/Electron Transport Complex IV,
http://linkedlifedata.com/resource/pubmed/chemical/Free Radicals,
http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide,
http://linkedlifedata.com/resource/pubmed/chemical/Iron,
http://linkedlifedata.com/resource/pubmed/chemical/Nitroblue Tetrazolium,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthine,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthine Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Xanthines
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
34
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
13802-10
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:7577973-Carbon Monoxide,
pubmed-meshheading:7577973-Circular Dichroism,
pubmed-meshheading:7577973-Copper,
pubmed-meshheading:7577973-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:7577973-Electron Transport,
pubmed-meshheading:7577973-Electron Transport Complex IV,
pubmed-meshheading:7577973-Free Radicals,
pubmed-meshheading:7577973-Hydrogen Peroxide,
pubmed-meshheading:7577973-Hydrogen-Ion Concentration,
pubmed-meshheading:7577973-Iron,
pubmed-meshheading:7577973-Models, Chemical,
pubmed-meshheading:7577973-Nitroblue Tetrazolium,
pubmed-meshheading:7577973-Oxidation-Reduction,
pubmed-meshheading:7577973-Spectrophotometry,
pubmed-meshheading:7577973-Superoxides,
pubmed-meshheading:7577973-Xanthine,
pubmed-meshheading:7577973-Xanthine Oxidase,
pubmed-meshheading:7577973-Xanthines
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pubmed:year |
1995
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pubmed:articleTitle |
The interaction of cytochrome oxidase with hydrogen peroxide: the relationship of compounds P and F.
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pubmed:affiliation |
Department of Biochemistry & Cell Biology, Rice University, Houston, Texas 77251-1892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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