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Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

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Published on: January 16, 2016

Guidelines for tunneling in enzymes.

Christopher C Moser1, J L Ross Anderson, P Leslie Dutton

  • 1Dept. Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, PA 19104, USA. moserc@mail.med.upenn.edu

Biochimica Et Biophysica Acta
|May 13, 2010
PubMed
Summary
This summary is machine-generated.

This study quantifies sequential oxidation-reduction rates in enzymes, identifying risks for nicotinamides and guiding the design of new artificial oxidoreductases with tailored redox engineering.

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Area of Science:

  • Biochemistry
  • Bioinorganic Chemistry
  • Enzyme Engineering

Background:

  • Oxidoreductases utilize single-electron-tunneling chains for redox reactions.
  • Quantifying multi-electron transfer is crucial for understanding enzyme mechanisms and designing artificial systems.

Purpose of the Study:

  • To extend existing models for single-electron tunneling to quantify sequential oxidation-reduction rates of multi-electron cofactors and substrates.
  • To identify conditions under which nicotinamides are susceptible to radical-mediated oxidation-reduction.
  • To provide a framework for designing novel artificial oxidoreductases.

Main Methods:

  • Merging electron-tunneling expressions with Eyring's chemical rate expressions.
  • Developing quantitative models for sequential electron transfer in enzymatic systems.

Main Results:

  • Established a method to quantify sequential oxidation-reduction rates for two-or-more electron cofactors and substrates.
  • Identified specific vulnerabilities of nicotinamides to radical-mediated redox processes.
  • Developed a theoretical basis for independent design and redox engineering of artificial oxidoreductases.

Conclusions:

  • The developed framework enables precise prediction and control of redox reaction rates in enzymatic and artificial systems.
  • This research facilitates the rational design of artificial oxidoreductases with tunable redox properties.
  • Understanding nicotinamide redox chemistry is advanced, with implications for enzyme stability and function.