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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1977-12-29
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pubmed:abstractText |
When ferricytochrome c is reduced by H atoms (produced by pulse radiolysis) at neutral pH where it is in a closed protein configuration, a considerable percentage of the reduction proceeds through electron equivalent transfer via the protein. At pH 2.0, where cytochrome c is in an open configuration, H atoms reduce by adding directly to the heme porphyrin. The intermediate then observed is identified through similarity with that formed on ferriheme alone.
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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:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
12
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pubmed:volume |
462
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pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
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pubmed:pagination |
161-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:20947-Cytochrome c Group,
pubmed-meshheading:20947-Electron Transport,
pubmed-meshheading:20947-Hydrogen-Ion Concentration,
pubmed-meshheading:20947-Kinetics,
pubmed-meshheading:20947-Oxidation-Reduction,
pubmed-meshheading:20947-Protein Conformation,
pubmed-meshheading:20947-Spectrum Analysis,
pubmed-meshheading:20947-Structure-Activity Relationship
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pubmed:year |
1977
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pubmed:articleTitle |
Conformation-dependent participation of the protein in electron equivalent transfer to cytochrome c.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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