Protonmotive activity of cytochrome c oxidase: control of oxidoreduction of the heme centers by the protonmotive force in the reconstituted beef heart enzyme-Reference-Cited by-同舟云学术

Protonmotive activity of cytochrome c oxidase: control of oxidoreduction of the heme centers by the protonmotive force in the reconstituted beef heart enzyme

Published:1990-03-01 Issue:12 Volume:29 Page:2939-2945
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Capitanio Nazzareno,De Nitto Emanuele,Villani Gaetano,Capitanio Giuseppe,Papa Sergio

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00464a008

Reference44 articles.

1. Involvement of intramitochondrial protons in redox reactions of cytochromea

2. Spectroelectrochemical study of cytochrome c oxidase: pH and temperature dependences of the cytochrome potentials. Characterization of site-site interactions.

3. Functional intermediates of cytochrome oxidase. Role of “pulsed” oxidase in the pre-steady state and steady state reactions of the beef enzyme.

4. Limited-turnover studies on proton translocation in reconstituted cytochrome c oxidase-containing vesicles

5. Dicyclohexylcarbodiimide binds specifically and covalently to cytochrome c oxidase while inhibiting its H+-translocating activity.

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