Photolabeling on beta -subunit of the nucleotide site related to hysteretic inhibition of mitochondrial F sub(1)-ATPase

While F sub(1)-ATPase can hydrolyze about any nucleoside triphosphate, it can undergo a hysteretic inhibition only in the presence of nucleotides or analogues bearing an adenine ring. This difference in specificity has been used to identify the location of the regulatory site in F sub(1)-ATPase. 3&#...

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Bibliographic Details
Published inBiochemistry (Easton) Vol. 23; no. 22; pp. 5294 - 5299
Main Authors Fellous, G, Godinot, C, Baubichon, H, Di Pietro, A, Gautheron, D C
Format Journal Article
LanguageEnglish
Published 01.01.1984
Subjects
coupling factor 1
mitochondria
nucleotides
photoaffinity labelling
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Summary:While F sub(1)-ATPase can hydrolyze about any nucleoside triphosphate, it can undergo a hysteretic inhibition only in the presence of nucleotides or analogues bearing an adenine ring. This difference in specificity has been used to identify the location of the regulatory site in F sub(1)-ATPase. 3'-O-(3-(N-(4-azido-2-nitrophenyl)amino)propionyl)adenosine 5'-diphosphate (NAP sub(3)-ADP) behaves as ADP to induce the hysteretic inhibition of F sub(1)-ATPase. The radioactive analogue also binds to F sub(1)-ATPase with the same stoichiometry and the same concentration dependence as ADP. It is therefore an excellent photoaffinity label to localize the regulatory site. Catalytic sites being occupied by guanosine 5'-( beta , gamma -imidotriphosphate), the photoirradiation-induced covalent binding of NAP sub(3)-ADP to the beta -subunit of F sub(1)-ATPase can be directly related to the hysteretic inhibition.
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ISSN:0006-2960