Activation volumes in enzymic catalysis: their sources and modification by low molecular weight solutes

P. S. Low, G. N. Somero

Research output: Contribution to journalArticle

100 Scopus citations

Abstract

Changes in enzyme conformation are often accompanied by large changes in volume. Model compound studies suggest that these volume changes may derive from two sources: (i) 'hydration density' effects due to changes in the exposure to solvent of protein groups which modify water density, and (ii) 'structural' contributions arising from changes in the volume of the protein itself. An experimental approach was developed to test the validity of the predictions based on model compound studies for catalytic conformational changes. By examining the effects of different solutes on the activation volumes of different enzymic reactions, we show that both sources of volume change provide significant contributions to the activation volume.

Original languageEnglish (US)
Pages (from-to)3014-3018
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume72
Issue number8
DOIs
StatePublished - 1975

ASJC Scopus subject areas

  • General

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