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- W2019227144 abstract "F <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>1</sub> -ATPase, a rotary motor enzyme, can catalyse ATP hydrolysis in which the central γ-subunit ratates inside the α <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>3</sub> β <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>3</sub> cylinder. Here, a four-state catalytic model of F <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>1</sub> -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 F <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>1</sub> -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 F <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>1</sub> -ATPase is also affected apparently, and the external torque which decreases the mean ratation rate of the F <sub xmlns:mml=http://www.w3.org/1998/Math/MathML xmlns:xlink=http://www.w3.org/1999/xlink>1</sub> motor to zero equals to the constant one which is produced during the ratation of the motor." @default.
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- W2019227144 date "2010-06-01" @default.
- W2019227144 modified "2023-09-23" @default.
- W2019227144 title "The Catalytic Mechanism Based on a Four-State Model of F1-ATPase" @default.
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- W2019227144 doi "https://doi.org/10.1109/icbbe.2010.5515835" @default.
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