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Dissecting hydrogen bond energetics to answer the age-old question: “How much do hydrogen bonds contribute to enzymatic catalysis?”

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This research investigates how much hydrogen bonds contribute to enzymatic catalysis, particularly in ketosteroid isomerase.
Evaluated hydrogen bond energetics using linear free energy relationships in ketosteroid isomerase.
Compared internal hydrogen bond donors to water molecules in analogous nonenzymatic reactions.
Assessed multiple models and environments surrounding the enzyme active site.
KSI's active site hydrogen bond donors are stronger than analogous water molecules, enhancing catalytic effect.
Evidence against distinct enzyme environments improving hydrogen bond energetics compared to aqueous solutions was found.
Quantitative models estimate the contribution of hydrogen bonds to catalysis across other enzymes, indicating broader applicability.

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Randomized trial quantifies hydrogen bond contributions to catalysis in enzymes, suggesting new mechanisms for enhancement.

Pinney et al. (2026) studied this question.

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