A chemical thermodynamic model of motor enzymes unifies chemical-Fx and powerstroke models.
A chemical thermodynamic model of motor enzymes unifies chemical-Fx and powerstroke models.
复制标题
DOI:
10.1016/j.bpj.2022.02.034
复制
发表时间:
2022-04-05
影响因子:
3.4
通讯作者:
Baker, Josh E.
中科院分区:
文献类型:
--
作者:
Baker, Josh E.
Molecular motors play a central role in many biological processes, ranging from pumping blood and breathing to growth and wound healing. Through motor-catalyzed chemical reactions, these nanomachines convert the chemical free energy from ATP hydrolysis into two different forms of mechanical work. Motor enzymes perform reversible work, wrev, through an intermediate step in their catalyzed reaction cycle referred to as a working step, and they perform Fx work when they move a distance, x, against a force, F. In a powerstroke model, wrev is performed when the working step stretches a spring within a given motor enzyme. In a chemical-Fx model, wrev is performed in generating a conserved Fx potential defined external to the motor enzyme. It is difficult to find any common ground between these models even though both have been shown to account for mechanochemical measurements of motor enzymes with reasonable accuracy. Here, I show that, by changing one simple assumption in each model, the powerstroke and chemical-Fx model can be reconciled through a chemical thermodynamic model. The formal and experimental justifications for changing these assumptions are presented. The result is a unifying model for mechanochemical coupling in motor enzymes first presented by A.V. Hill in 1938 that is consistent with single-molecule structural and mechanical data.
登录
查看更多内容
影响因子:
2.9
作者:
LYMN, RW;TAYLOR, EW
通讯作者:
TAYLOR, EW
影响因子:
3.4
作者:
Astumian, R. Dean
通讯作者:
Astumian, R. Dean
影响因子:
3.4
作者:
Baker, JE;Brosseau, C;Warshaw, DM
通讯作者:
Warshaw, DM
影响因子:
64.8
作者:
FINER, JT;SIMMONS, RM;SPUDICH, JA
通讯作者:
SPUDICH, JA
DOI:
10.1073/pnas.95.6.2944
发表时间:
1998-03-17
影响因子:
11.1
作者:
Baker, JE;Brust-Mascher, I;Thomas, DD
通讯作者:
Thomas, DD