Simple models for extracting mechanical work from the ATP hydrolysis cycle.
According to the binding-zipper model, the RecA class of ATPase motors converts chemical energy into mechanical force by the progressive annealing of hydrogen bonds between the nucleotide and the catalytic pocket. The role of hydrolysis is to weaken the binding of products, allowing them to be released so that the cycle can repeat. Molecular dynamics can be used to study the unbinding process, but the binding process is more complex, so that inferences about it are made indirectly from structural, mutation, and biochemical studies. Here we present a series of models of varying complexity that illustrate the basic processes involved in force production during ATP binding. These models reveal the role of solvent and geometry in determining the amount of mechanical work that can be extracted from the binding process.
Department of Chemical Engineering, University of California, Berkeley, California, USA.
Jonathan L
JL
Eide
Arup K
AK
Chakraborty
George F
GF
Oster
D000251:Adenosine Triphosphatases / Q000737:chemistry / Q000502:physiology; D000255:Adenosine Triphosphate / Q000737:chemistry* / Q000502:physiology*; D001665:Binding Sites; D001696:Biomechanical Phenomena / Q000379:methods; D003198:Computer Simulation; D004548:Elasticity; D004735:Energy Transfer / Q000502:physiology*; D006868:Hydrolysis; D008954:Models, Biological; D008956:Models, Chemical; D020409:Molecular Motor Proteins / Q000737:chemistry* / Q000502:physiology*; D009038:Motion; D009068:Movement / Q000502:physiology; D011485:Protein Binding; D015398:Signal Transduction / Q000502:physiology; D013314:Stress, Mechanical
D020409:Molecular Motor Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases