Electric Fields and Enzyme Catalysis.

Author: Fried SD1, Boxer SG2
Affiliation:
1Proteins and Nucleic Acid Chemistry Division, Medical Research Council Laboratory of Molecular Biology, Cambridge CB2 0QH, United Kingdom; email: sf537@cam.ac.uk.
2Department of Chemistry, Stanford University, Stanford, California 94305; email: sboxer@stanford.edu.
Conference/Journal: Annu Rev Biochem.
Date published: 2017 Jun 20
Other: Volume ID: 86 , Pages: 387-415 , Special Notes: doi: 10.1146/annurev-biochem-061516-044432. Epub 2017 Mar 24. , Word Count: 155


What happens inside an enzyme's active site to allow slow and difficult chemical reactions to occur so rapidly? This question has occupied biochemists' attention for a long time. Computer models of increasing sophistication have predicted an important role for electrostatic interactions in enzymatic reactions, yet this hypothesis has proved vexingly difficult to test experimentally. Recent experiments utilizing the vibrational Stark effect make it possible to measure the electric field a substrate molecule experiences when bound inside its enzyme's active site. These experiments have provided compelling evidence supporting a major electrostatic contribution to enzymatic catalysis. Here, we review these results and develop a simple model for electrostatic catalysis that enables us to incorporate disparate concepts introduced by many investigators to describe how enzymes work into a more unified framework stressing the importance of electric fields at the active site.

KEYWORDS: electric fields; enzyme electrostatics; infrared spectroscopy; preorganization; protein biophysics; vibrational Stark effect

PMID: 28375745 DOI: 10.1146/annurev-biochem-061516-044432

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