The nonexistence of specially stabilized hydrogen bonds in enzymes

S Scheiner, T Kar - Journal of the American Chemical Society, 1995 - ACS Publications
S Scheiner, T Kar
Journal of the American Chemical Society, 1995ACS Publications
Ab initio calculations are used to test a recent suggestion that enzymic catalysis can be
aidedby strengthening of a hydrogen bond in a key intermediate, occurring when this bond
is shortened and the pKa's of the two groups are equalized. The requisite amount of energy
is not available in electrically neutral H-bonds; no additional strengthening can be
accomplished by shortening such a bond. Interaction energies where one subunit is
charged, on the other hand, can be very high. These bonds are intrinsically veryshort, and …
Abstract
Ab initio calculations are used to test a recent suggestion that enzymic catalysis can be aidedby strengthening of a hydrogen bond in a key intermediate, occurring when this bond is shortened and the pKa’s of the two groups are equalized. The requisite amount of energy is not available in electrically neutral H-bonds; no additional strengthening can be accomplished by shortening such a bond. Interaction energies where one subunit is charged, on the other hand, can be very high. These bonds are intrinsically veryshort, and the proton transfer profile contains a very low energy barrier. There is no special stabilization associated with the disappearance of the transferbarrier or equalization of the pKa’s.
ACS Publications
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