DocumentCode
3107985
Title
The Catalytic Mechanism Based on a Four-State Model of F1-ATPase
Author
Wu Weixia ; Zhan Yong ; Han Yingrong ; Chen Yafei
Author_Institution
Sci. Educ. Dept., Beijing Inst. of Graphic Commun., Beijing, China
fYear
2010
fDate
18-20 June 2010
Firstpage
1
Lastpage
4
Abstract
F1-ATPase, a rotary motor enzyme, can catalyse ATP hydrolysis in which the central γ-subunit ratates inside the α3β3 cylinder. Here, a four-state catalytic model of F1-ATPase is studied in which we think that the ATP hydrolysis and synthesis are ATP-dependent and ADP/Pi-dependent, respectively. The results show that the catalytic ratation mechanism of F1-ATPase is affected distinctly by the ATP/ADP/Pi concentrations. The model accords well with the expermental observations. Moreover, when the external load exists, the mean rotation rate of F1-ATPase is also affected apparently, and the external torque which decreases the mean ratation rate of the F1 motor to zero equals to the constant one which is produced during the ratation of the motor.
Keywords
biochemistry; catalysis; enzymes; molecular biophysics; physiological models; α3β3 cylinder; ATP-ADP-Pi concentrations; F1-ATPase; catalyse ATP hydrolysis; catalytic mechanism; catalytic ratation mechanism; central γ-subunit ratates; external torque; four-state model; mean ratation rate; rotary motor enzyme; Biochemistry; Biophysics; Educational technology; Energy conversion; Engine cylinders; Graphics; Microorganisms; Proteins; Shafts; Torque;
fLanguage
English
Publisher
ieee
Conference_Titel
Bioinformatics and Biomedical Engineering (iCBBE), 2010 4th International Conference on
Conference_Location
Chengdu
ISSN
2151-7614
Print_ISBN
978-1-4244-4712-1
Electronic_ISBN
2151-7614
Type
conf
DOI
10.1109/ICBBE.2010.5515835
Filename
5515835
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