Abstract:
:Bovine heart cytochrome-c oxidase was reconstituted in liposomes and the kinetics of cytochrome c oxidation were measured by the polarographic and photometric method under uncoupled conditions in the presence of various polyvalent anions. In order to distinguish between specific and unspecific ionic effects of ATP, the photolabelling reagent 8-azido-ATP was applied. Covalently bound ATP at the enzyme complex caused the same increase of Km for cytochrome c as free ATP, if measured by the photometric assay. The increase of Km by photolabelling with 8-azido-ATP was completely prevented by ATP, but not by ADP. The data indicate the occurrence of a specific binding site for ATP at the cytosolic side of cytochrome-c oxidase, which, after binding of ATP, changes the kinetics of cytochrome c oxidation.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Hüther FJ,Kadenbach Bdoi
10.1016/0014-5793(86)80018-7subject
Has Abstractpub_date
1986-10-20 00:00:00pages
89-94issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(86)80018-7journal_volume
207pub_type
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