Drobinskaya I Y, Kozlov I A, Murataliev M B, Vulfson E N
FEBS Lett. 1985 Mar 25;182(2):419-24. doi: 10.1016/0014-5793(85)80346-x.
The binding of one ADP molecule at the catalytic site of the nucleotide depleted F1-ATPase results in a decrease in the initial rate of ATP hydrolysis. The addition of an equimolar amount of ATP to the nucleotide depleted F1-ATPase leads to the same effect, but, in this case, inhibition is time dependent. The half-time of this process is about 30 s, and the inhibition is correlated with Pi dissociation from the F1-ATPase catalytic site (uni-site catalysis). The F1-ATPase-ADP complex formed under uni-site catalysis conditions can be reactivated in two ways: (i) slow ATP-dependent ADP release from the catalytic site (tau 1/2 20 s) or (ii) binding of Pi in addition to MgADP and the formation of the triple F1-ATPase-MgADP-Pi complex. GTP and GDP are also capable of binding to the catalytic site, however, without changes in the kinetic properties of the F1-ATPase. It is proposed that ATP-dependent dissociation of the F1-ATPase-GDP complex occurs more rapidly, than that of the F1-ATPase-ADP complex.
一个ADP分子结合在核苷酸耗尽的F1 - ATP酶的催化位点会导致ATP水解初始速率降低。向核苷酸耗尽的F1 - ATP酶中添加等摩尔量的ATP会产生相同的效果，但在这种情况下，抑制作用是时间依赖性的。这个过程的半衰期约为30秒，并且抑制作用与磷酸根从F1 - ATP酶催化位点解离相关（单位点催化）。在单位点催化条件下形成的F1 - ATP酶 - ADP复合物可以通过两种方式重新激活：（i）ATP依赖的ADP从催化位点缓慢释放（半衰期为20秒），或（ii）除了MgADP之外磷酸根的结合以及形成三元F1 - ATP酶 - MgADP - 磷酸根复合物。GTP和GDP也能够结合到催化位点，然而，F1 - ATP酶的动力学性质没有变化。有人提出，F1 - ATP酶 - GDP复合物的ATP依赖解离比F1 - ATP酶 - ADP复合物的解离更快。
