8 May 1989 Raman Difference Spectroscopy And The Energetics Of Enzymatic Catalysis
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Proceedings Volume 1057, Biomolecular Spectroscopy; (1989) https://doi.org/10.1117/12.951658
Event: OE/LASE '89, 1989, Los Angeles, CA, United States
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.
© (1989) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Robert Callender, Robert Callender, Hua Deng, Hua Deng, Donald Sloan, Donald Sloan, John Burgner, John Burgner, Kwok To Yue, Kwok To Yue, "Raman Difference Spectroscopy And The Energetics Of Enzymatic Catalysis", Proc. SPIE 1057, Biomolecular Spectroscopy, (8 May 1989); doi: 10.1117/12.951658; https://doi.org/10.1117/12.951658

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