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Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors

Ye Gao, Björn Meyer, Lucie Sokolova, Klaus Zwicker, Michael Karas, Bernd Brutschy, Guohong Peng and Hartmut Michel
Proceedings of the National Academy of Sciences of the United States of America
Vol. 109, No. 9 (February 28, 2012), pp. 3275-3280
Stable URL: http://www.jstor.org/stable/41506941
Page Count: 6
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Heme-copper terminal oxidase using both cytochrome c and ubiquinol as electron donors
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Abstract

The cytochrome c oxidase Cox2 has been purified from native membranes of the hyperthermophilic eubacterium Aquifex aeolicus. It is a cytochrome ba₃ oxidase belonging to the family B of the heme-copper containing terminal oxidases. It consists of three subunits, subunit I (CoxA2,63.9 kDa), subunit II (CoxB2,16.8 kDa), and an additional subunit IIa of 5.2 kDa. Surprisingly it is able to oxidize both reduced cytochrome c and ubiquinol in a cyanide sensitive manner. Cox2 is part of a respiratory chain supercomplex. This supercomplex contains the fully assembled cytochrome bc₁ complex and Cox2. Although direct ubiquinol oxidation by Cox2 conserves less energy than ubiquinol oxidation by the cytochrome bc₁ complex followed by cytochrome c oxidation by a cytochrome c oxidase, ubiquinol oxidation by Cox2 is of advantage when all ubiquinone would be completely reduced to ubiquinol, e.g., by the sulfide: quinone oxidoreductase, because the cytochrome bc₁ complex requires the presence of ubiquinone to function according to the Q-cycle mechanism. In the case that all ubiquinone has been reduced to ubiquinol its reoxidation by Cox2 will enable the cytochrome bc₁ complex to resume working.

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