| Literature DB >> 2848497 |
A Reimann1, F J Hüther, J A Berden, B Kadenbach.
Abstract
The biphasic effect of anions on the activity of isolated bovine heart cytochrome c oxidase is paralleled by changes in the visible oxidized spectra, indicating the different conformational changes in the enzyme induced by bromide, chloride, sulphate, phosphate, ADP and ATP. Photoaffinity-labelling of most subunits of the isolated enzyme by low concentrations of 8-azido-[gamma-32P]ATP is strongly increased by ATP, ADP and unlabelled 8-azido-ATP in an unspecific manner. With the reconstituted enzyme less subunits are labelled and this labelling is only little affected by nucleotides. The data suggest a highly dynamic structure for isolated bovine heart cytochrome c oxidase.Entities:
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Year: 1988 PMID: 2848497 PMCID: PMC1135144 DOI: 10.1042/bj2540723
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857