ATP Binding to Bovine Heart Cytochrome C Oxidase. A Photoaffinity Labelling Study

Overview

Journal Biochem J

Specialty Biochemistry

Date 1986 Feb 15

PMID 3010954

Citations 12

Authors

C Montecucco

G Schiavo

R Bisson

Affiliations

Soon will be listed here.

Abstract

ATP influences the kinetic properties of cytochrome c oxidase. A photoactivatable radioactive ATP analogue was used to localize the nucleotide-binding site on the bovine heart enzyme. Subunits IV and VIII were specifically labelled, suggesting that these two nuclear-coded polypeptides may play a regulatory role on the oxidase functions.

Citing Articles

Revisiting Kadenbach: Electron flux rate through cytochrome c-oxidase determines the ATP-inhibitory effect and subsequent production of ROS.

Vogt S, Rhiel A, Weber P, Ramzan R Bioessays. 2016; 38(6):556-67.

PMID: 27171124 PMC: 5084804. DOI: 10.1002/bies.201600043.

Tissue-specific regulation of bovine heart cytochrome-c oxidase activity by ADP via interaction with subunit VIa.

Anthony G, Reimann A, KADENBACH B Proc Natl Acad Sci U S A. 1993; 90(5):1652-6.

PMID: 8383320 PMC: 45937. DOI: 10.1073/pnas.90.5.1652.

Nuclear-encoded subunits of human cytochrome c oxidase: SstI restriction fragment length polymorphism.

Adjoa S, Bouchard C, Coetzer P, Noakes T, Dionne F Hum Genet. 1994; 93(3):347-8.

PMID: 7907316 DOI: 10.1007/BF00212037.

ATP-induced spectral changes in cytochrome c oxidase. A kinetic investigation.

Antonini G, Malatesta F, Sarti P, Vallone B, Brunori M Biochem J. 1988; 256(3):835-40.

PMID: 2852006 PMC: 1135491. DOI: 10.1042/bj2560835.

Influence of 8-azido-ATP and other anions on the activity of cytochrome c oxidase.

Huther F, Berden J, KADENBACH B J Bioenerg Biomembr. 1988; 20(4):503-16.

PMID: 2851591 DOI: 10.1007/BF00762206.

References

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