Literature DB >> 9739469

Cytochrome c oxidase from eucaryotes but not from procaryotes is allosterically inhibited by ATP.

K Follmann1, S Arnold, S Ferguson-Miller, B Kadenbach.   

Abstract

The activity of reconstituted cytochrome c oxidase from bovine heart but not from Rhodobacter sphaeroides is allosterically inhibited by intraliposomal ATP, which binds to subunit IV. The activity of cytochrome c oxidase of wild-type yeast and of a subunit VIa-deleted yeast mutant, measured with Tween 20-solubilized mitochondria in the presence of an ATP-regenerating system, was also allosterically inhibited by ATP, indicating the general validity of this mechanism of "respiratory control" in eucaryotic cytochrome c oxidases (Arnold and Kadenbach, Eur. J. Biochem. (1997) 249, 350-354). Deletion of subunit VIa changes the biphysic into monophysic kinetics of the yeast enzyme in the presence of ADP. A tenfold higher amount of horse heart cytochrome c, as compared to yeast cytochrome c, was required to relieve the ATP inhibition of the yeast enzyme.

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Year:  1998        PMID： 9739469     DOI： 10.1002/iub.7510450522

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN： 1039-9712


  8 in total

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