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Proceedings Paper

Raman Difference Spectroscopy And The Energetics Of Enzymatic Catalysis
Author(s): Robert Callender; Hua Deng; Donald Sloan; John Burgner; Kwok To Yue
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Paper Abstract

Typically, there are specific molecular interactions between a substrate and enzyme, which occur during enzymatic catalysis, that must be sufficient to not only reduce the transition state barrier appropriate for the reaction but also define a particular (usually small) set of chemical reactions. Both the origins and strengths of these interactions are fundamental issues in understanding how enzymes work. While more structural information is increasingly available from X-ray crystallographic studies, the extent of these interactions and the electronic character of the substrate and nearby protein groups within the active site generally must be simply surmised from the structural data and kinetic studies. Rarely are these molecular properties directly measured. We have approached this problem by determining the vibrational spectra of bound substrates using Raman spectroscopy. The observed vibrational frequencies are a measure of force constants between particular atoms, and these constants can be related in turn to bond orders and electronic distributions between these atoms.

Paper Details

Date Published: 8 May 1989
PDF: 7 pages
Proc. SPIE 1057, Biomolecular Spectroscopy, (8 May 1989); doi: 10.1117/12.951658
Show Author Affiliations
Robert Callender, The City University of New York (United States)
Hua Deng, The City University of New York (United States)
Donald Sloan, The City University of New York (United States)
John Burgner, Purdue University (United States)
Kwok To Yue, Emory University (United States)

Published in SPIE Proceedings Vol. 1057:
Biomolecular Spectroscopy
Robert R. Birge; Henry H. Mantsch, Editor(s)

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