A Study of the Mechanism of Electron Transfer in Cytochrome c
| Autor: | Arthur Kowalsky |
|---|---|
| Rok vydání: | 1969 |
| Předmět: |
inorganic chemicals
Cytochrome biology Cytochrome c peroxidase Cytochrome c Inorganic chemistry technology industry and agriculture chemistry.chemical_element Cell Biology Phosphate Dithionite Biochemistry chemistry.chemical_compound Chromium chemistry otorhinolaryngologic diseases biology.protein Cytochrome c oxidase Ferricyanide Molecular Biology |
| Zdroj: | Journal of Biological Chemistry. 244:6619-6625 |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(18)63451-9 |
| Popis: | Cytochrome c is swiftly and quantitatively reduced by chromous ion. In the course of the reduction chromium is bound to the protein. At pH 4.78 and 7.0 the ratio of chromium to cytochrome c is approximately 0.5 mole per mole. When phosphate is present during the reduction, the ratio increases to approximately unity, and 1 mole of phosphate is also bound. The chromium-ferrocytochrome c complex can be reoxidized with ferricyanide with little loss of chromium and can be reduced again with dithionite. However, if chromous ion is used to reduce ferricytochrome c-chromium, only partial reduction occurs. The cytochrome c-chromium-phosphate complex is active with cytochrome oxidase and with the cytochrome c reductase of a bovine heart submitochondrial preparation. In the latter system, however, rates are markedly lower. The cytochrome c-chromium-phosphate complex has been digested with pepsin, and a crude fraction has been isolated which still contains iron, chromium, and phosphate. |
| Databáze: | OpenAIRE |
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