Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins.

ABSTRACT: Some oxidoreductase enzymes use redox-active tyrosine, tryptophan, cysteine, and/or glycine residues as one-electron, high-potential redox (radical) cofactors. Amino-acid radical cofactors typically perform one of four tasks-they work in concert with a metallocofactor to carry out a multielectron redox process, serve as storage sites for oxidizing equivalents, activate the substrate molecules, or move oxidizing equivalents over long distances. It is challenging to experimentally resolve the thermodynamic and kinetic redox properties of a single-amino-acid residue. The inherently reactive and highly oxidizing properties of amino-acid radicals increase the experimental barriers further still. This review describes a family of stable and well-structured model proteins that was made specifical

SUBMITTER: Tommos C 

PROVIDER: S-EPMC9922538 | biostudies-literature | 2022 May

REPOSITORIES: biostudies-literature