Properties of the Cytochrome c Oxidase Activity of Cytochrome b_<561> from Photoanaerobically Grown Rhodopseudomonas sphaeroides
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概要
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Cytochrome b_<561> from Rhodopseudomonas sphaeroids had cytochrome c (c_2) oxidase activity and a pH optimum at 6.0 for this activity. The activity was affected by the ionic strength of the reaction mixture. The apparent Km and maximal velocity (V_<max>) values in the absence of added salts were 14 μM and 120 nmol oxidized per min per mg protein for horse heart cytochrome c. Reduced horse heart cytochrome c was reoxidized in first-order kinetics by this cytochrome b_<561>. The specific activity was 0.7 s^<-1> per mg protein at 20℃ at the concentration of 30 μM cytochrome c. Activity was inhibited by KCN and NaN_3, but not by antimycin. The addition of a low concentration of KCN to the cytochrome b_<561> produced a change in the absorption spectrum, evidence that KCN interacts with the heme moiety of cytochrome b_<561> Results of this and preceeding studies show that the cytochrome oxidase (cytochrome "o" ) described earlier (Sasaki et al. 1970) is cytochrome b_<561>.
- 日本植物生理学会の論文
著者
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Takamiya Ken-ichiro
Department of Biological Sciences, Faculty of Bioscience and Biotechnology, Tokyo Institute of Techn
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Takamiya Ken-ichiro
Department Of Biological Sciences Faculty Of Bioscience And Biotechnology
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