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Chemistry

How ATP Hydrolysis Drives Thermodynamically Unfavorable Biosynthetic Reactions

Quick fact

ATP hydrolysis can drive biosynthetic reactions because, when coupled, the favorable energy release of ATP breakdown (ΔG ≈ -30 kJ/mol in cells) is combined with the unfavorable reaction's energy requirement, making the overall ΔG negative. Enzymes achieve this by binding both ATP and the reactant in a single active site, forming a phosphorylated intermediate.

Why this is interesting

You know ATP is the 'energy currency' of the cell. But how can a single molecule of ATP, just sitting in the cytoplasm, pay for building a complex molecule like a protein? The answer is chemical coupling.