The complex of mitochondrial F1‐ATPase with the natural inhibitor protein is unable to catalyze single‐site ATP hydrolysis

FEBS Letters

Milgrom, Ya.M.¹  Postanogova, N.V.¹  Kalashnikova, T.Yu.¹ 

[1] A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, 119899 Moscow, USSR

关键词: F1-ATPase;    Inhibitor protein;    Single-site catalysis;    IP;    natural inhibitor protein of mitochondrial F1-ATPase;    BSA;    bovine serum albumin;   

DOI  :  10.1016/0014-5793(88)80663-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Interaction of mitochondrial F₁-ATPase with the isolated natural inhibitor protein resulting in the inhibition of multi-site ATP hydrolysis is accompanied by the loss of activity at low ATP concentrations when single-site hydrolysis should occur. Catalytic site occupancy by [¹⁴C]nucleotides in F₁-ATPase during steady-state [¹⁴C]ATP hydrolysis, which is saturated in parallel with single-site catalysis, is prevented after blocking the enzyme with the inhibitor protein.

【 授权许可】

Unknown