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Photolabeling on beta subunit of the nucleotide site related to hysteretic inhibition of mitochondrial f 1 atpase



Photolabeling on beta subunit of the nucleotide site related to hysteretic inhibition of mitochondrial f 1 atpase



Biochemistry 23(22): 5294-5299



While F1-ATPase can hydrolyze about any nucleoside triphosphate, it can undergo a hysteretic inhibition only in the presence of nucleotides or analogs bearing an adenine ring. This difference in specificity was used to identify the location of the regulatory site in F1-ATPase. 3'-O-[3-[N-(4-Azido-2-nitrophenyl)amino]propionyl]adenosine 5'-diphosphate (NAP3-ADP) behaves as ADP to induce the hysteretic inhibition of F1-ATPase. The radioactive analog also binds to F1-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 NAP3-ADP to the .beta.-subunit of F1-ATPase can be directly related to the hysteretic inhibition. On the contrary, there is no correlation between the inhibition of ATPase activity and the limited binding of NAP3-ADP to the .alpha.-subunit. Therefore, the regulatory site must be located on the .beta.-subunit of the mitochondrial F1-ATPase.

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Accession: 006110915

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