JMB-HEADER RAS-JOURNALS EIMB Pleiades Publishing

RUS

             

ENG

YearIMPACT-FACTOR
2021  1,540
2020  1,374
2019  1,023
2018  0,932
2017  0,977
2016  0,799
2015  0,662
2014  0,740
2013  0,739
2012  0,637
2011  0,658
2010  0,654
2009  0,570
2008  0,849
2007  0,805
2006  0,330
2005  0,435
2004  0,623
2003  0,567
2002  0,641
2001  0,490
2000  0,477
1999  0,762
1998  0,785
1997  0,507
1996  0,518
1995  0,502
Vol 46(2012) N 5 p. 710-716;
B.N. Goldstein, A.M. Aksirov*, D.T. Zakrjevskaia

Irregular Activity Oscillations of a Rotary Molecular Motor: A Simple Kinetic Model of F1-ATPase

Institute of Theoretical and Experimental Biophysics, Russian Academy of Sciences, Pushchino, Moscow Region, 142290 Russia

*konf1@rambler.ru
Received - 2011-12-06; Accepted - 2011-12-23

F1-ATPase is a catalytic part of the F1Fo-ATP synthase molecular motor. The cooperative hydrolysis of ATP at three catalytic sites of F1-ATPase is accompanied by the rotation of the central γ-subunit inside a cylinder formed by three α-subunits and three β-subunits. Experimental works of different authors have shown that the γ-subunit rotates with irregular dwells. A simple kinetic model suggested in this article provides an explanation as to why dwells occur during the rotation of F1-ATPase. According to this model, rotation dwells happen as a result of deterministic chaos, which in turn occurs at rate constants that are close to those demonstrated experimentally. The time duration of dwells in the model is in agreement with that observed experimentally. Our model explains the known irregular occupan cy of catalytic sites of F1-ATPase by nucleotides.

F1-ATPase rotary motor, kinetic model, deterministic chaos



JMB-FOOTER RAS-JOURNALS