Postanogova N V
A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, USSR.
FEBS Lett. 1988 Mar 28;230(1-2):163-6. doi: 10.1016/0014-5793(88)80663-x.
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.
线粒体F1-ATP酶与分离出的天然抑制蛋白相互作用，导致多位点ATP水解受到抑制，同时在应发生单位点水解的低ATP浓度下活性丧失。在稳态[14C]ATP水解过程中，F1-ATP酶中[14C]核苷酸占据催化位点，该过程与单位点催化同时达到饱和，但在用抑制蛋白阻断酶后，这种占据被阻止。
