Abstract
In eukaryotic cells as well as in some bacteria, ATP is created using a splendid molecular machine–FoF1-ATP synthase . It synthesizes ATP from ADP (adenosine di-phosphate) and Pi (a phosphate group) by consuming the proton motive force generated by respiration in mitochondria, photolysis in chloroplast and photosynthetic bacteria, or even glycolysis in several bacteria. In some cases, it also hydrolyzes ATP to maintain the proton gradient across the membrane. F0F1-ATP synthase contains two parts, F1 and F0. The focus here is on the thermodynamics and kinetics of ATP hydrolysis and synthesis F0F1-ATP synthase, as well as on the recent efforts in identifying the nucleotide-binding site by linking the available experimental thermodynamic and structural information with the help of molecular dynamic simulations. The thermodynamics of HTP hydrolysis and ATP synthesis is given in detail. The description given here of the current understanding being achieved for F1-ATPase by both theoretical and experimental advances is expected to be of use in the analysis of other motor proteins, with examples. Computational and theoretical studies at the different levels of detail can make important contributions to understand these systems.
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