Adirect measurement of the standard freeâenergy change associated with the hydrolysis of atp is technically demanding because the minute amount of atp remaining at equilibrium is difficult to measure accurately. the value of î g â² â can be calculated indirectly, however, from the equilibrium constants of two other enzymatic reactions having less favorable equilibrium constants:
keil-270 k. g2=890 glucose 6-phosphate+ h2o â glucose+ p, eq1 atp + glucose â adp+ glucose 6-phosphate using this information for equilibrium constants determined at 25 "c, calculate the standard free energy of hydrolysis of atp