If ATP is the free energy "currency" of a cell, how does a cell synthesize a compound (such as creatine phosphate) with a much higher phosphate transfer potential than that of ATP?
First,
values for ATP
hydrolysis do not represent actual
G' values
under likely biological conditions. ATP has a considerably higher
G' value at intracellular concentrations of
ATP, ADP, and AMP than it has under standard conditions.
For example, consider the following reaction, catalyzed by creatine kinase:
Creatine + ATP <=> Creatine Phosphate + ADP.
This reaction is endergonic (
= +12 kcal/mol)
under standard conditions but, because ATP levels are very high
within mitochondria, and creatine phosphate levels are relatively
low, the reaction is exergonic as written and proceeds to the
right. Thus, the cellular concentration of metabolites has a drastic
effect on the free energy for a reaction, enabling ATP to create
phosphorylated compounds with higher phosphoryl transfer potential
than itself under standard conditions.