Question

1. Why does hydrogenation of ATP have high barrier (mostly doesn't happen spontaneous in typical biological conditions) compared to hydrogenation of OH- (does happen spontaneously). Both contain Oxygen atom with one covalent bond and -1 formal charge. One would naively expect the two reaction have similar properties.

2. Is the reaction product of hydrolysis of ATP somehow high in energy, while water is low in energy? Does the phosphates somehow magically make the reaction barrier higher?

Answer 1

The hydrolysis of ATP releases a large amount of free energy, making it a high-energy molecule. The presence of phosphate groups in ATP allows it to perform cellular work. The hydrolysis of OH- happens spontaneously in biological conditions.

Step-by-step explanation:

The hydrolysis of ATP releases a large amount of free energy, making it a high-energy molecule. This is due to the high-energy bonds between the phosphate groups in ATP, which are broken during hydrolysis. The release of free energy during ATP hydrolysis fuels many cellular processes and reactions.

In contrast, the hydrolysis of OH- does not require the breaking of high-energy bonds and therefore happens spontaneously in typical biological conditions.

The reaction product of hydrolysis of ATP, which is ADP and Pi, is lower in energy than ATP. Water, on the other hand, is lower in energy. The presence of phosphate groups in ATP does not magically make the reaction barrier higher, but rather the release of free energy during ATP hydrolysis allows it to perform cellular work.