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Science 24 June 1994:
Vol. 264. no. 5167, pp. 1927 - 1930
DOI: 10.1126/science.7661899
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Articles

Science, Vol 264, Issue 5167, 1927-1930
Copyright © 1994 by American Association for the Advancement of Science

articles

A low-barrier hydrogen bond in the catalytic triad of serine proteases

PA Frey, SA Whitt, and JB Tobin

Institute for Enzyme Research, Graduate School, University of Wisconsin at Madison 53705.

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.


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