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STUDIES ON CYTOCHROME b-563 OF KLEBSIELLA RHINOSCLEROMATIS II PHYSICO-CHEMICAL PROPERTIES AND BIOLOGICAL ACTIVITY.

By using ferricyanide-ferrocyanide system, the oxidation-reduction potential of cytochrome b-563 at pH 7.0, 30℃ was found to be +0.127 volts. After successive dialysis against 10~(-4)M EDTA and then redistilled water, the purified cytochrome b-563 was found to contain 0.28% iron. The minimal molecular weight thus calculated was 20,000. The millimolar extinction coefficients at 563,533 and 430 nm were calculated to be 35.1, 20.1 and 197.5 mM~(-1) cm~(-1) respectively. The spectra of both the reduced and the oxidized cytochrome b-563 were not altered by CO or cyanide. Cytochrome b-563 was autooxidizable. In the presence of K. rhinoscleromatis particulate fraction, cytochrome b-563 could be reduced by NADH, lactic acid, formic acid and succinio acid, the relative activities in decreasing order were as follows: 1.6, 1.5, 1.24 and 1.0. These demonstrated that cytochrome b-563 was biologically active. The prosthetic group of cytochrome b-563 was identified as protoheme on the basis of its spectral characteristics, paper chromatographic behavior and reconstitution experiment. Cytochrome b-563 could be reconstituted from the apoprotein and its prosthetic group. The spectral characteristics of the reconstituted cytochrome b-563 was the same as those of the original pigment. The reconstitution of the pigment was not inhibited by 5×10~(-4)M p-chloromercuribenzoate, which suggested that sulfhydryl groups were not involved in the binding between protoheme and the protein moiety. The reconstituted cytochrome b-563 could also be reduced by lactic acid in the presence of K. rhinoscleromatis particulate fraction under anaerobic conditions, but the relative activity was only 27% as that of the original cytochrome b-563. These results suggested that the binding between protoheme and the protein moiety was somewhat altered by the acid-acetone splitting procedure.