Thermodynamics of the hydrolysis of adenosine 5'-triphosphate to adenosine 5'-diphosphate Export

@article{Gajewski86, abstract = {The enthalpy of hydrolysis of the enzyme-catalyzed (heavy meromyosin) conversion of adenosine 5'-triphosphate (ATP) to adenosine 5'-diphosphate (ADP) and inorganic phosphate has been investigated using heat-conduction microcalorimetry. Enthalpies of reaction were measured as a function of ionic strength (0.05-0.66 mol kg-1), pH (6.4-8.8), and temperature (25-27°C) in Tris/HCl buffer. The measured enthalpies were adjusted for the effects of proton ionization and metal ion binding, protonation and interaction with the Tris buffer, and ionic strength effects to obtain a value of ?H0 = -20.5 ± 0.4 kJ mol-1 at 25°C for the process, ATP4-(aq) + H2O(l) = ADP3-(aq) + HPO42-(aq) + H+(aq), where aq is aqueous and l is liquid. Heat measurements carried out at different temperatures lead to a value of ?C(p)0 = -237 ± 30 kJ mol-1 K-1 for the above process.}, address = {Chemical Thermodynamics Division, National Bureau of Standards, Gaithersburg, MD 20899, United States}, author = {Gajewski, E. and Steckler, D. K. and Goldberg, R. N.}, citeulike-article-id = {1572695}, citeulike-linkout-0 = {http://www.scopus.com/record/display.url?view=extended&origin=resultslist&eid=2-s2.0-0022970054}, journal = {J. Biol. Chem.}, keywords = {adp, atp, hydrolysis}, number = {27}, pages = {12733--12737}, posted-at = {2007-08-17 17:29:11}, priority = {2}, title = {Thermodynamics of the hydrolysis of adenosine 5'-triphosphate to adenosine 5'-diphosphate}, url = {http://www.scopus.com/record/display.url?view=extended&origin=resultslist&eid=2-s2.0-0022970054}, volume = {261}, year = {1986} }

TY - JOUR ID - Gajewski86 L3 - citeulike-article-id:1572695 N2 - The enthalpy of hydrolysis of the enzyme-catalyzed (heavy meromyosin) conversion of adenosine 5'-triphosphate (ATP) to adenosine 5'-diphosphate (ADP) and inorganic phosphate has been investigated using heat-conduction microcalorimetry. Enthalpies of reaction were measured as a function of ionic strength (0.05-0.66 mol kg-1), pH (6.4-8.8), and temperature (25-27°C) in Tris/HCl buffer. The measured enthalpies were adjusted for the effects of proton ionization and metal ion binding, protonation and interaction with the Tris buffer, and ionic strength effects to obtain a value of ?H0 = -20.5 ± 0.4 kJ mol-1 at 25°C for the process, ATP4-(aq) + H2O(l) = ADP3-(aq) + HPO42-(aq) + H+(aq), where aq is aqueous and l is liquid. Heat measurements carried out at different temperatures lead to a value of ?C(p)0 = -237 ± 30 kJ mol-1 K-1 for the above process. IS - 27 JF - J. Biol. Chem. AD - Chemical Thermodynamics Division, National Bureau of Standards, Gaithersburg, MD 20899, United States EP - 12737 TI - Thermodynamics of the hydrolysis of adenosine 5'-triphosphate to adenosine 5'-diphosphate VL - 261 SP - 12733 KW - adp KW - atp KW - hydrolysis AU - Gajewski, E AU - Steckler, DK AU - Goldberg, RN PY - 1986/// UR - http://www.scopus.com/record/display.url?view=extended&origin=resultslist&eid=2-s2.0-0022970054 ER -