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• W2067887310 startingPage "1887" @default.
• W2067887310 abstract "Formation of a short (less than 2.5 angstroms), very strong, low-barrier hydrogen bond in the transition state, or in an enzyme-intermediate complex, can be an important contribution to enzymic catalysis. Formation of such a bond can supply 10 to 20 kilocalories per mole and thus facilitate difficult reactions such as enolization of carboxylate groups. Because low-barrier hydrogen bonds form only when the pKa's (negative logarithm of the acid constant) of the oxygens or nitrogens sharing the hydrogen are similar, a weak hydrogen bond in the enzyme-substrate complex in which the pKa's do not match can become a strong, low-barrier one if the pKa's become matched in the transition state or enzyme-intermediate complex. Several examples of enzymatic reactions that appear to use this principle are presented." @default.
• W2067887310 created "2016-06-24" @default.
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• W2067887310 date "1994-06-24" @default.
• W2067887310 modified "2023-10-17" @default.
• W2067887310 title "Low-Barrier Hydrogen Bonds and Enzymic Catalysis" @default.
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• W2067887310 doi "https://doi.org/10.1126/science.8009219" @default.
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