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• W2022106218 endingPage "543" @default.
• W2022106218 startingPage "533" @default.
• W2022106218 abstract "Reduction of cytochrome aa3 in proteoliposomes with ascorbate plus cytochrome c confirms that not more than 55% of the molecules are externally accessible and that the remainder are reduced only on the addition of membrane-permeable N,N,N′,N′tetramethyl-p-henylenediamine. Reduction in the presence of terminal inhibitors such as cyanide, azide, and carbon monoxide shows that likewise 50% of the cytochrome a is accessible and 50% inaccessible. Dithionite reduces part of the cytochrome a3 in the presence of azide, and none in the presence of cyanide. Methyl viologen, which is somewhat membrane permeable, can reduce part of the cyanide-complexed cytochrome a3 at low concentrations and all of it at high concentrations. Cytochrome a3 is therefore also distributed randomly inside and outside the vesicles. Cytochrome c oxidase with externally facing cytochrome a is stimulated to high activity by its membrane association. Its turnover is dependent on the external pH and it is inhibited by external azide; trapping of azide cannot be used to demonstrate the orientation of the cytochrome a3 hemes associated with externally facing cytochrome a. Cytochrome c oxidase with internally facing cytochrome a is rather sluggishly reactive. Its low activity accounts for the apparent failure of detergents to release extra activity on lysing proteoliposomes. Double reciprocal plots of the reaction of added cytochrome c with proteoliposomes indicate apparent biphasic binding in the energized state, which is abolished upon the addition of uncouplers and valinomycin. But no transmembraneous effect upon the oxidase reaction other than energization has been identified." @default.
• W2022106218 created "2016-06-24" @default.
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• W2022106218 date "1980-10-01" @default.
• W2022106218 modified "2023-09-25" @default.
• W2022106218 title "Orientation and reactivity of cytochrome aa3 heme groups in proteoliposomes" @default.
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• W2022106218 doi "https://doi.org/10.1016/0003-9861(80)90065-x" @default.
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