Computing Proton-Coupled Redox Potentials of Fluorotyrosines in a Protein Environment.

ABSTRACT: The oxidation of tyrosine to form the neutral tyrosine radical via proton-coupled electron transfer is essential for a wide range of biological processes. The precise measurement of the proton-coupled redox potentials of tyrosine (Y) in complex protein environments is challenging mainly because of the highly oxidizing and reactive nature of the radical state. Herein, a computational strategy is presented for predicting proton-coupled redox potentials in a protein environment. In this strategy, both the reduced Y-OH and oxidized Y-O^• forms of tyrosine are sampled with molecular dynamics using a molecular mechanical force field. For a large number of conformations, a quantum mechanical/molecular mechanical (QM/MM) electrostatic embedding scheme is used to compute the free-e

SUBMITTER: Reinhardt CR 

PROVIDER: S-EPMC8045599 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature