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Theoretical studies on substrate binding to the active site of carbonic anhydrase
Author(s) -
Sawaryn Andrzej,
Andrzej Sokalski W.
Publication year - 1979
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560160211
Subject(s) - chemistry , active site , cndo/2 , histidine , carbonic anhydrase , carbonic anhydrase ii , computational chemistry , carbonic acid , stereochemistry , molecule , catalysis , enzyme , organic chemistry
The role of some amino acids and metal ions in the catalytic activity of carbonic anhydrase (carbonate dehydratase EC 4.2.1.1) has been investigated. The additional stabilization of the transition state complex was used as the qualitative measure of the effect of molecular surrounding on CO 2 hydration reaction calculated within the approximate CNDO /2 approach. The effect of the molecular environment has been simulated by inclusion into the SCF LCAO MO Hamiltonian, a term representing the interaction with a set of point charges and atomic dipoles centered on experimentally determined position of Zn 2+ ion and all atoms of histidine 94, 96, 119 and threonine 199, 200 (or histidine 200 in the case of carbonic anhydrase B). The possible molecular mechanism of CO 2 hydration inside the active site has been also discussed.