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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
|
| pubmed:dateCreated |
1995-4-11
|
| pubmed:abstractText |
Cytochrome c is one of the most thoroughly documented oxidoreduction proteins. Its electron transfer activity, which involves an association between the heme group and the polypeptidic chain, is correlated with the redox potential value of the heme group. The redox potential covers a wide range up to 0.8 V, an extreme case being observed in the low-potential cytochromes c from sulfate reducing bacteria. On of the main roles of the polypeptidic moiety consists of modulating the redox potential value of the heme group. In this paper, some structural factors that seem likely to be involved in maintaining the redox potential value are described.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0300-9084
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
76
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
471-9
|
| pubmed:dateRevised |
2005-11-16
|
| pubmed:meshHeading | |
| pubmed:year |
1994
|
| pubmed:articleTitle |
The protein moiety modulates the redox potential in cytochromes c.
|
| pubmed:affiliation |
Unité de Bioénergétique et Ingénierie des Protéines, CNRS, Marseille, France.
|
| pubmed:publicationType |
Journal Article,
Review
|