Nonempirical Analysis of the Nature of Catalytic Effects in Ribonuclease A Active Site

Published

April 30, 2001

Author(s)

P Kedzierski, W A. Sokalski, Morris Krauss

Abstract

The physical nature of the catalytic activity exerted by various ribonuclease A active site constituents is analyzed in terms of the differential transition state stabilization approach in which activation barrier changes induced by the molecular environment are expressed by additive components defined in the theory of intermolecular interactions. Electrostatic multipole contributions seem to approximate total catalytic activity well for residues separated by contacts longer than 2.7 whereas at shorter distances the remaining exchange and delocalization terms are not negligible. Depending on the reaction step, the same residue may exhibit catalytic or inhibitory activity.Differential Transition State Stabilization approach, where activation barrier changes induced by molecular environment are expressed by additive components defined in the theory of intermolecular interactions. Electrostatic multipole contributions seem to approximate total catalytic activity well for residues separated by contacts longer than 2.7 A, whereas at shorter distances remaining exchange and delocalization terms are not negligible. Depending on the reaction step, the same residue may exhibit catalytic or inhibitory activity

Citation

Journal of Computational Chemistry

Volume

21

Issue

6

Pub Type

Journals

Keywords

active site, catalytic activity, electrostatic effects, intermolecular interactions, ribonuclease A

Citation

Kedzierski, P. , Sokalski, W. and Krauss, M. (2001), Nonempirical Analysis of the Nature of Catalytic Effects in Ribonuclease A Active Site, Journal of Computational Chemistry (Accessed December 30, 2024)