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Catalytic efficiency of dehaloperoxidase A is controlled by electrostatics - application of the vibrational Stark effect to understand enzyme kinetics
Citation key Schkolnik2013
Author Schkolnik, Gal and Utesch, Tillmann and Zhao, Junjie and Jiang, Shu and Thompson, Matthew K. and Mroginski, Maria-Andrea and Hildebrandt, Peter and Franzen, Stefan
Pages 1011–1015
Year 2013
DOI 10.1016/j.bbrc.2012.12.047
Journal Biochemical and Biophysical Research Communications
Volume 430
Number 3
Month jan
Abstract The vibrational Stark effect is gaining popularity as a method for probing electric fields in proteins. In this work, we employ it to explain the effect of single charge mutations in dehaloperoxidase-hemoglobin A (DHP A) on the kinetics of the enzyme. In a previous communication published in this journal (BBRC 2012, 420, 733-737) it has been shown that an increase in the overall negative charge of DHP A through mutation causes a decrease in its catalytic efficiency. Here, by labeling the protein with 4-mercaptobenzonitrile (MBN), a Stark probe molecule, we provide further evidence that the diffusion control of the catalytic process arises from the electrostatic repulsion between the enzyme and the negatively charged substrate. The linear correlation observed between the nitrile stretching frequency of the protein-bound MBN and the catalytic efficiency of the single-site mutants of the enzyme indicates that electrostatic interactions play a dominant role in determining the catalytic efficiency of DHP A. (C) 2012 Elsevier Inc. All rights reserved.
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