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Features of Organization and Mechanism of Catalysis of Two Families of Terminal Oxidases: Heme-Copper and bd-Type

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Abstract

Terminal oxidases of aerobic respiratory chains catalyze the transfer of electrons from the respiratory substrate, cytochrome c or quinol, to O2 with the formation of two H2O molecules. There are two known families of these membrane oxidoreductases: heme-copper oxidase superfamily and bd-type oxidase family (cytochromes bd) found in prokaryotes only. The redox reaction catalyzed by these enzymes is coupled to the generation of proton motive force used by the cell to synthesize ATP and to perform other useful work. Due to the presence of the proton pump, heme-copper oxidases create the membrane potential with a greater energy efficiency than cytochromes bd. The latter, however, play an important physiological role that enables bacteria, including pathogenic ones, to survive and reproduce under adverse environmental conditions. This review discusses the features of organization and molecular mechanisms of functioning of terminal oxidases from these two families in the light of recent experimental data.

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Abbreviations

BNC:

binuclear center

COX:

cytochrome oxidase

HCO:

heme-copper oxidase

PLS:

proton-loading site

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Acknowledgements

The authors are grateful to V. P. Skulachev, A. A. Konstantinov, and A. D. Vinogradov for their interest in this work, useful discussion, and critical remarks.

Funding

This work was supported by the Russian Science Foundation (project 19-14-00063).

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  1. Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, 119991, Moscow, Russia

    V. B. Borisov & S. A. Siletsky

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  1. V. B. Borisov
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Correspondence to V. B. Borisov.

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This article does not contain any studies involving animals or human participants performed by any of the authors.

Published in Russian in Biokhimiya, 2019, Vol. 84, No. 11, pp. 1718–1732.

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Borisov, V.B., Siletsky, S.A. Features of Organization and Mechanism of Catalysis of Two Families of Terminal Oxidases: Heme-Copper and bd-Type. Biochemistry Moscow 84, 1390–1402 (2019). https://doi.org/10.1134/S0006297919110130

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