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Tightly bound nucleotides affect phosphate binding to mitochondrial F 1 ‐ATPase
Author(s) -
Kozlov I.A.,
Vulfson E.N.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80347-1
Subject(s) - nucleotide , phosphate , atpase , chemistry , biophysics , biochemistry , v atpase , affect (linguistics) , microbiology and biotechnology , biology , enzyme , psychology , communication , gene
The interaction of inorganic phosphate with native and nucleotide‐depleted F 1 ‐ATPase was studied. F 1 ‐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 F 1 ‐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 F 1 ‐ATPase in the ATP synthesis reaction.