A Low-Barrier Hydrogen Bond in the Catalytic Triad of Serine Proteases
- 24 June 1994
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 264 (5167), 1927-1930
- https://doi.org/10.1126/science.7661899
Abstract
Spectroscopic properties of chymotrypsin and model compounds indicate that a low-barrier hydrogen bond participates in the mechanism of serine protease action. A low-barrier hydrogen bond between N delta 1 of His57 and the beta-carboxyl group of Asp102 in chymotrypsin can facilitate the formation of the tetrahedral adduct, and the nuclear magnetic resonance properties of this proton indicate that it is a low-barrier hydrogen bond. These conclusions are supported by the chemical shift of this proton, the deuterium isotope effect on the chemical shift, and the properties of hydrogen-bonded model compounds in organic solvents, including the hydrogen bond in cis-urocanic acid, in which the imidazole ring is internally hydrogen-bonded to the carboxyl group.Keywords
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