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ATP synthesis and hydrolysis in submitochondrial particles subjected to an acid—base transition
Author(s) -
Husain Iqbal,
Harris David A.
Publication year - 1983
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(83)80947-8
Subject(s) - submitochondrial particle , inhibitor protein , atp hydrolysis , atpase , chemistry , hydrolysis , biochemistry , phosphorylation , uncoupling agents , biophysics , mitochondrion , enzyme , biology
ATP hydrolysis or succinate oxidation by inhibitor‐rich submitochondrial particles leads to a 3‐fold increase in ATPase activity, with concomitant loss of about 30% of bound inhibitor protein. An acid—base transition causes similar, but smaller, effects (a 30% ATPase increase, and a loss of 8% of the inhibitor). Omitting the electrical component of the gradient completely abolished these effects. The inhibitor protein inhibits ADP phosphorylation induced by an acid—base transition but not by NADH oxidation. This is suggested to reflect the slow movement of the inhibitor protein and the brief period of acid—base jump phosphorylation.