Abstract
Monomeric cytochrome f from Japanese radish (Raphanus sativus L. var acanthiformis Makino) leaves was isolated in a homogeneous state with an A420.5/A277 of 7.6. Radish cytochrome f is a single polypeptide chain with a molecular weight of about 33,000. The midpoint potential is 350 mV. The amino acid analysis indicates the existence of 3 residues of half-cystine. Radish cytochrome f contains one thiol group which reacts with 5,5'-dithiobis(2-nitrobenzoic acid) only after denaturation by sodium dodecyl sulfate. Ferricytochrome f is reduced by the superoxide radical at the rate of 6 X 10(6) M-1 s-1 at pH 7.8. Radish ferricytochrome f is also reduced slowly without an exogenous electron donor. A kinetic study and the effect of the thiol reagent indicate that the autoreduction is an intramolecular reaction and that the thiol group is an electron donor.
Keywords
Affiliated Institutions
Related Publications
Studies on Cytochrome c Peroxidase
The stoichiometry of the reaction of cytochrome c peroxidase with hydrogen peroxide, and of the resulting Compound ES with both ferrocyanide and ferrocytochrome c as donor has b...
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +/- 0.1...
Publication Info
- Year
- 1978
- Type
- article
- Volume
- 253
- Issue
- 20
- Pages
- 7397-7403
- Citations
- 39
- Access
- Closed
External Links
Social Impact
Social media, news, blog, policy document mentions
Citation Metrics
Cite This
Identifiers
- DOI
- 10.1016/s0021-9258(17)34514-3