Conformational switching at cytochrome a during steady-state turnover of cytochrome c oxidase.

Abstract:

:As an electron transfer-driven proton pump, cytochrome c oxidase (ferrocytochrome-c:oxygen oxidoreductase, EC 1.9.3.1) must alternate between two conformations in each valence state of the redox element associated with ion translocation. Using second derivative absorption spectroscopy, the conformation of the cytochrome a cofactor has been investigated during steady-state turnover of this enzyme. Resting cytochrome c oxidase displays a transition for ferric cytochrome a at 430 nm. During aerobic steady-state turnover, this band is replaced by a ferrous cytochrome a transition at 450 nm. When anaerobicity is achieved, the transition occurs at 444 nm. The 450-nm-absorbing species is thus the dominant form during turnover, suggesting that conformational transitions of cytochrome a direct electron transfer during catalysis and may direct as well proton translocation in the last step of the respiratory electron transfer chain.

authors

Copeland RA

doi

10.1073/pnas.88.16.7281

keywords:

subject

Has Abstract

pub_date

1991-08-15 00:00:00

pages

7281-3

issue

16

eissn

0027-8424

issn

1091-6490

journal_volume

88

pub_type

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