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Impact of Hydrogen Bonding on the Susceptibility of Peptides to Oxidation
Author(s) -
Chan Bun,
Moran Damian,
Easton Christopher J.,
Radom Leo
Publication year - 2017
Publication title -
chemistry – an asian journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.18
H-Index - 106
eISSN - 1861-471X
pISSN - 1861-4728
DOI - 10.1002/asia.201700492
Subject(s) - hydrogen bond , chemistry , hydrogen atom abstraction , oxidative phosphorylation , amide , solvent , hydrogen , acceptor , hydrogen atom , photochemistry , computational chemistry , molecule , organic chemistry , biochemistry , group (periodic table) , physics , condensed matter physics
Abstract The tendency of peptides to be oxidized is intimately connected with their function and even their ability to exist in an oxidative environment. Here we report high‐level theoretical studies that show that hydrogen bonding can alter the susceptibility of peptides to oxidation, with complexation to a hydrogen‐bond acceptor facilitating oxidation, and vice versa, impacting the feasibility of a diverse range of biological processes. It can even provide an energetically viable mechanistic alternative to direct hydrogen‐atom abstraction. We find that hydrogen bonding to representative reactive groups leads to a broad (≈400 kJ mol −1 ) spectrum of ionization energies in the case of model amide, thiol and phenol systems. While some of the oxidative processes at the extreme ends of the spectrum are energetically prohibitive, subtle environmental and solvent effects could potentially mitigate the situation, leading to a balance between hydrogen bonding and oxidative susceptibility.