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Cytochrome c oxidase: understanding nature's design of a proton pump

Chan, Sunney I. and Li, Peter Mark (1990) Cytochrome c oxidase: understanding nature's design of a proton pump. Biochemistry, 29 (1). pp. 1-12. ISSN 0006-2960. doi:10.1021/bi00453a001.

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It has been estimated that nearly 90% of the O_2 consumed by aerobic organisms participates in the dioxygen chemistry of cytochrome c oxidase and becomes reduced to water in the terminal step of respiration. Cytochrome oxidases of the aa_3 type (having two a-type cytochromes) are found in a wide variety of aerobic organisms including bacteria, fungi, single- celled eukaryotes, plants, and animals. It is an integral membrane protein complex comprised of 2 or 3 subunits in the simplest bacterial systems and as many as 13 dissimilar subunits in mammals [for a review, see Wikström et al. (1981)].

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Chan, Sunney I.0000-0002-5348-2723
Additional Information:© 1990 American Chemical Society. Received June 16, 1989; Revised Manuscript Received July 17, 1989. This work was supported by Grant GM 22432 from the National Institute of General Medical Sciences, U.S. Public Health Service. Acknowledgement is made to the donors of the Petroleum Research Fund, administered by the American Chemical Society, for partial support.
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NIHGM 22432
American Chemical Society Petroleum Research FundUNSPECIFIED
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Caltech Arthur Amos Noyes Laboratory of Chemical Physics7961
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Official Citation:Cytochrome c oxidase: understanding nature's design of a proton pump. Sunney I. Chan and Peter Mark Li. Biochemistry 1990 29 (1), 1-12. DOI: 10.1021/bi00453a001
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:83042
Deposited By: Tony Diaz
Deposited On:07 Nov 2017 23:28
Last Modified:15 Nov 2021 19:54

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