Dynamics and kinetics of enzymes. Kinetic equilibrium of forces in biochemistry.
To explain the high specificity, high reaction rate, and high thermodynamic efficiency in enzymatic processes, cooperation of the enzyme with a molecular transfer unit is assumed. A "kinetic equilibrium of forces" is suggested, which enables high reaction rates to occur under equilibrium conditions and a thorough examination of the substrate to be made without consumption of free energy. In case of ATPases, ion-binding proteins are the most probable transfer units. By analyzing the elementary effect in muscle contraction it is shown that the new theorem may be of substantial value in elucidating biochemical processes.
Becker
E W
EW
Institute fur Mikrostrukturtechnik der Universitat Karlsrube, Bundesrepublik Deutschland.
D000199:Actins / Q000378:metabolism; D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000818:Animals; D001671:Biochemistry / Q000379:methods; D004798:Enzymes / Q000378:metabolism*; D007700:Kinetics; D008954:Models, Biological; D008962:Models, Theoretical; D009119:Muscle Contraction / Q000502:physiology*; D009218:Myosins / Q000378:metabolism; D013816:Thermodynamics
D000199:Actins; D004798:Enzymes; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases; D009218:Myosins