Dupont Y
FEBS Lett. 1983 Sep 5;161(1):14-20. doi: 10.1016/0014-5793(83)80721-2.
The mechanism of free energy coupling in active transport is discussed with special reference to the sarcoplasmic reticulum Ca2+-ATPase. In the current working schemes for cation transport ATPases, free energy transduction is nearly always based on enzyme conformational changes. The principal objective of the present article is to examine whether recent experimental results on Ca2+-ATPase may in fact be better explained by assuming the existence of a direct chemiosmotic process. In the scheme proposed, free energy transduction between ATP and calcium is based on a transfer of solvation water between the acylphosphate bond and the bound calcium ions.
本文特别参照肌浆网Ca2 + -ATP酶,讨论了主动运输中自由能偶联的机制。在当前阳离子运输ATP酶的工作方案中,自由能转导几乎总是基于酶的构象变化。本文的主要目的是研究,假设存在直接的化学渗透过程,是否实际上能更好地解释最近关于Ca2 + -ATP酶的实验结果。在所提出的方案中,ATP和钙之间的自由能转导是基于酰基磷酸键和结合的钙离子之间溶剂化水的转移。