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EnglishA study is presented on the effect of zinc binding at the matrix side, on the proton pump of purified liposome reconstituted bovine heart cytochrome c oxidase (COV). Internally trapped Zn2+ resulted in 50% decoupling of the proton pump at level flow. Analysis of the pH dependence of inhibition by internal Zn2+ of proton release in the oxidative and reductive phases of the catalytic cycle of cytochrome c oxidase indicates that Zn2+ suppresses two of the four proton pumping steps in the cycle, those taking place when the 2 OH− produced in the reduction of O2 at the binuclear center are protonated to 2 H2O. This decoupling effect could be associated with Zn2+ induced conformational alteration of an acid/base cluster linked to heme a3.
Inhibition of proton pumping in membrane reconstituted bovine heart cytochrome c oxidase by zinc binding at the inner matrix side / P.L. MARTINO; CAPITANIO G; N. CAPITANIO; S. PAPA. - In: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS. - ISSN 0005-2728. - 1807(2011), pp. 1075-1082.
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| Titolo: | Inhibition of proton pumping in membrane reconstituted bovine heart cytochrome c oxidase by zinc binding at the inner matrix side |
| Autori: | |
| Data di pubblicazione: | 2011 |
| Rivista: | |
| Citazione: | Inhibition of proton pumping in membrane reconstituted bovine heart cytochrome c oxidase by zinc binding at the inner matrix side / P.L. MARTINO; CAPITANIO G; N. CAPITANIO; S. PAPA. - In: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS. - ISSN 0005-2728. - 1807(2011), pp. 1075-1082. |
| Abstract: | A study is presented on the effect of zinc binding at the matrix side, on the proton pump of purified liposome reconstituted bovine heart cytochrome c oxidase (COV). Internally trapped Zn2+ resulted in 50% decoupling of the proton pump at level flow. Analysis of the pH dependence of inhibition by internal Zn2+ of proton release in the oxidative and reductive phases of the catalytic cycle of cytochrome c oxidase indicates that Zn2+ suppresses two of the four proton pumping steps in the cycle, those taking place when the 2 OH− produced in the reduction of O2 at the binuclear center are protonated to 2 H2O. This decoupling effect could be associated with Zn2+ induced conformational alteration of an acid/base cluster linked to heme a3. |
| Handle: | http://hdl.handle.net/11586/10560 |
| Appare nelle tipologie: | 1.1 Articolo in rivista |
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