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Ingredients Necessary for Proton Transfer in Enzymes
Author(s) -
Scheiner Steve
Publication year - 2009
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1560/ijc.49.2.139
Subject(s) - chemistry , intramolecular force , proton , hydrogen bond , context (archaeology) , substrate (aquarium) , enzyme , serine , catalysis , ion , stereochemistry , dipole , crystallography , chemical physics , computational chemistry , molecule , biochemistry , organic chemistry , nuclear physics , paleontology , physics , oceanography , biology , geology
The transfer of a proton across a hydrogen bond can be influenced by a number of factors, including H‐bond length, intramolecular angles, and the presence of neighboring groups. The ability of different factors to push a proton across the H‐bond is examined for a specific and very important pair of catalytic groups, Ser‐195 and His‐57, within the context of a serine proteinase enzyme. The influence of residue Asp‐102 is considered for different charge states, as is the nature of the surrounding medium. Also examined are the perturbations introduced by the substrate and external ions and dipoles.