Energy Transfer from Adenosine Triphosphate Export

@article{citeulike:2290669, abstract = {Abstract: We suggest a direct molecular mechanism of energy transfer from adenosine triphosphate (ATP) in hydrolysis and phosphorylation reactions, from chemical energy into mechanical energy. Upon hydrolysis of ATP, say bound to a protein, the electrostatic energy of Coulombic repulsion of the ions adenosine diphosphate and phosphate is available to assert a force on a neighboring molecular group in the protein and can do work on that group, or as the ions recede from each without asserting such a force, they gain relative kinetic energy, which, in the absence of dissipative collisions that turn this kinetic energy into heat, can be converted into any other form of energy and work by an impulse, a collision with a neighboring group, without restrictions. Either possibility can be used as a source of activation energy for reactions, as a source of energy to surmount energy barriers in conformational changes, and as a source of work to be done, as in muscle. In some systems where the Gibbs free energy change is fully utilized, all of this energy is turned into mechanical energy, and we suggest a similar mechanism. From the literature we cite some experimental evidence and several quotations indicative of the possibility of our suggestion.}, address = {Department of Chemistry, Stanford University, Stanford, California 94305}, author = {Ross, J.}, citeulike-article-id = {2290669}, citeulike-linkout-0 = {http://dx.doi.org/10.1021/jp0556862}, citeulike-linkout-1 = {http://pubs.acs.org/doi/abs/10.1021/jp0556862}, day = {6}, doi = {10.1021/jp0556862}, journal = {J. Phys. Chem. B}, keywords = {coupling, vet, vibration}, month = {April}, number = {13}, pages = {6987--6990}, posted-at = {2009-02-12 00:32:25}, priority = {2}, title = {Energy Transfer from Adenosine Triphosphate}, url = {http://dx.doi.org/10.1021/jp0556862}, volume = {110}, year = {2006} }

TY - JOUR ID - citeulike:2290669 L3 - citeulike-article-id:2290669 N2 - Abstract: We suggest a direct molecular mechanism of energy transfer from adenosine triphosphate (ATP) in hydrolysis and phosphorylation reactions, from chemical energy into mechanical energy. Upon hydrolysis of ATP, say bound to a protein, the electrostatic energy of Coulombic repulsion of the ions adenosine diphosphate and phosphate is available to assert a force on a neighboring molecular group in the protein and can do work on that group, or as the ions recede from each without asserting such a force, they gain relative kinetic energy, which, in the absence of dissipative collisions that turn this kinetic energy into heat, can be converted into any other form of energy and work by an impulse, a collision with a neighboring group, without restrictions. Either possibility can be used as a source of activation energy for reactions, as a source of energy to surmount energy barriers in conformational changes, and as a source of work to be done, as in muscle. In some systems where the Gibbs free energy change is fully utilized, all of this energy is turned into mechanical energy, and we suggest a similar mechanism. From the literature we cite some experimental evidence and several quotations indicative of the possibility of our suggestion. IS - 13 JF - J. Phys. Chem. B AD - Department of Chemistry, Stanford University, Stanford, California 94305 EP - 6990 TI - Energy Transfer from Adenosine Triphosphate VL - 110 SP - 6987 KW - coupling KW - vet KW - vibration AU - Ross, J PY - 2006/04/06/ UR - http://dx.doi.org/10.1021/jp0556862 ER -