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FEBS Lett. 2008 Dec 24;582(30):4158-62. doi: 10.1016/j.febslet.2008.11.018. Epub 2008 Nov 28.

Inhibition of membrane-bound cytochrome c oxidase by zinc ions: high-affinity Zn2+-binding site at the P-side of the membrane.

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A.N. Belozersky Institute, M.V. Lomonosov Moscow State University, Moscow 119992, Russia.


In the presence of the uncoupler, external zinc ions inhibit rapidly turnover of cytochrome c oxidase reconstituted in phospholipid vesicles or bound to the membrane of intact mitochondria. The effect is promoted by electron leaks into the oxidase during preincubation with Zn(2+). Inhibition of liposome-bound bovine cytochrome oxidase by external Zn(2+) titrates with a K(i) of 1+/-0.3 microM. Presumably, the Zn(2+)-binding group at the positively charged side is not reactive in the oxidized enzyme, but becomes accessible to the cation in some partially reduced state(s) of the oxidase; reduction of Cu(B) is tentatively proposed to be responsible for the effect.

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