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X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O₂ activation and unidirectional proton-pump mechanisms.

ABSTRACT: Cytochrome c oxidase (CcO) reduces O₂ to water, coupled with a proton-pumping process. The structure of the O₂-reduction site of CcO contains two reducing equivalents, Fe _a₃²⁺ and Cu_B¹⁺, and suggests that a peroxide-bound state (Fe _a₃³⁺-O^--O^--Cu_B²⁺) rather than an O₂-bound state (Fe _a₃²⁺-O₂) is the initial catalytic intermediate. Unexpectedly, however, resonance Raman spectroscopy results have shown that the initial intermediate is Fe _a₃²⁺-O₂, whereas Fe _a₃³⁺-O^-<

SUBMITTER: Shimada A

PROVIDER: S-EPMC7186171 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature

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X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O₂ activation and unidirectional proton-pump mechanisms.

OmicsDI is part of the ELIXIR infrastructure

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X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O2 activation and unidirectional proton-pump mechanisms.

OmicsDI is part of the ELIXIR infrastructure

Tweets

X-ray structures of catalytic intermediates of cytochrome c oxidase provide insights into its O₂ activation and unidirectional proton-pump mechanisms.