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The pKavalue of His 57-Asp 102 couple in the active site of bovine pancreatic β-trypsin: A molecular orbital study

Authors
Journal
Journal of Theoretical Biology
0022-5193
Publisher
Elsevier
Publication Date
Volume
99
Issue
4
Identifiers
DOI: 10.1016/0022-5193(82)90196-5
Disciplines
  • Biology

Abstract

Abstract The charge relay hypothesis generated a large number of theoretical and experimental studies that tested the ideas involved. Opinion based upon theoretical and experimental studies is divided on the prediction, although there are many experimental data which do not support the hypothesis. The essential feature is the proton transfer from the histidine imidazole to the aspartate. Thus, we have performed the detailed calculations of the proton transfer from His 57 to Asp 102 including the environment of the couple in protonated bovine pancreatic β-trypsin. The charge state of the His 57-Asp 102 couple is greatly influenced by the environment of the enzyme around it. In this paper, it is shown that the proton between His 57 and Asp 102 is covalently bonded to the His 57 imidazole in the protonated β-trypsin. Our MO calculations, which support the neutral-pK-histidine theory as the results, do not support the charge relay mechanism.

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