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

ChemistryCytochrome cCytochromeThiolSodium dodecyl sulfateMonomerRaphanusStereochemistryPhotochemistryBiochemistryOrganic chemistryEnzymeMitochondrion

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Year
1978
Type
article
Volume
253
Issue
20
Pages
7397-7403
Citations
39
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Keiji Tanaka, Masaaki Takahashi, Kozi Asada (1978). Isolation of monomeric cytochrome f from Japanese radish and a mechanism of autoreduction.. Journal of Biological Chemistry , 253 (20) , 7397-7403. https://doi.org/10.1016/s0021-9258(17)34514-3

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DOI
10.1016/s0021-9258(17)34514-3