منابع مشابه
Kinetics and chemomechanical properties of the F1-ATPase molecular motor
F1-ATPase hydrolyzes ATP into ADP and Pi and converts chemical energy into mechanical rotation with exceptionally high efficiency. This energy-transducing molecular motor increasingly attracts interest for its unique cellular functions and promising application in nanobiotechnology. To better understand the chemomechanics of rotation and loading dynamics of F1-ATPase, we propose a computational...
متن کاملPhosphoenzymes formed from Mg.ATP and Ca.ATP during pre-steady state kinetics of sarcoplasmic reticulum ATPase.
We have investigated here the pre-steady state kinetics of sarcoplasmic reticulum ATPase incubated under conditions where significant amounts of Mg.ATP and Ca.ATP coexist, both of them being substrates for the ATPase. We confirmed that these two substrates are independently hydrolyzed by the ATPase, which thus apparently catalyzes Pi production by two simultaneous and separate pathways. Externa...
متن کاملSteady-state and pre-steady-state kinetics of the mitochondrial F(1)F(o) ATPase: is ATP synthase a reversible molecular machine?
H(+)-ATP synthase (F(1)F(o) ATPase) catalyzes the synthesis and/or hydrolysis of ATP, and the reactions are strongly affected by all the substrates (products) in a way clearly distinct from that expected of a simple reversibly operating enzyme. Recent studies have revealed the structure of F(1), which is ideally suited for the alternating binding change mechanism, with a rotating gamma-subunit ...
متن کاملA model for the cooperative free energy transduction and kinetics of ATP hydrolysis by F1-ATPase.
Although the binding change mechanism of rotary catalysis by which F1-ATPase hydrolyzes ATP has been supported by equilibrium, kinetic, and structural observations, many questions concerning the function remain unanswered. Because of the importance of this enzyme, the search for a full understanding of its mechanism is a key problem in structural biology. Making use of the results of free energ...
متن کاملAnalytical Solution of Steady State Substrate Concentration of an Immobilized Enzyme Kinetics by Laplace Transform Homotopy Perturbation Method
The nonlinear dynamical system modeling the immobilized enzyme kinetics with Michaelis-Menten mechanism for an irreversible reaction without external mass transfer resistance is considered. Laplace transform homotopy perturbation method is used to obtain the approximate solution of the governing nonlinear differential equation, which consists in determining the series solution convergent to the...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: FEBS Letters
سال: 1985
ISSN: 0014-5793
DOI: 10.1016/0014-5793(85)80056-9