Published January 9, 1990
| public
Journal Article
Cytochrome c oxidase: understanding nature's design of a proton pump
- Creators
-
Chan, Sunney I.
- Li, Peter Mark
Abstract
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)].
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.Additional details
- Eprint ID
- 83042
- Resolver ID
- CaltechAUTHORS:20171107-152051230
- GM 22432
- NIH
- American Chemical Society Petroleum Research Fund
- Created
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2017-11-07Created from EPrint's datestamp field
- Updated
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2021-11-15Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Arthur Amos Noyes Laboratory of Chemical Physics
- Other Numbering System Identifier
- 7961