Tightly bound nucleotides affect phosphate binding to mitochondrial F1‐ATPase

FEBS Letters

Kozlov, I.A.¹  Vulfson, E.N.¹ 

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

关键词: Mitochondrial F1-ATPase;    Phosphate binding;    Nucleotide binding;   

DOI  :  10.1016/0014-5793(85)80347-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The interaction of inorganic phosphate with native and nucleotide-depleted F₁-ATPase was studied. F₁-ATPase depleted of tightly bound nucleotides loses the ability to bind inorganic phosphate. The addition of ATP, ADP, GTP and GDP but not AMP, restores the phosphate binding. The nucleotides affecting the phosphate binding to F₁-ATPase are located at the catalytic (exchangeable) site of the enzyme. The phosphate is thought to bind to the same catalytic site where the nucleotide is already bound. It is thought that ADP is the first substrate to bind to F₁-ATPase in the ATP synthesis reaction.

【 授权许可】

Unknown