• 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