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Annual Review of Biophysics

Volume 51, 2022

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 specifically to study tyrosine and tryptophan oxidation-reduction. The so-called αX model protein system was combined with very-high-potential protein film voltammetry, transient absorption spectroscopy, and theoretical methods to gain a comprehensive description of the thermodynamic and kinetic properties of protein tyrosine and tryptophan radicals.

Keyword(s): amino-acid radical, glycyl radical enzymes, hole hopping, proton-coupled electron transfer, radical transfer, tryptophan radical, tyrosine radical
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/content/journals/10.1146/annurev-biophys-100521-103031
2022-05-09
2024-05-29
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/content/journals/10.1146/annurev-biophys-100521-103031
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Insights into the Thermodynamics and Kinetics of Amino-Acid Radicals in Proteins
Annual Review of Biophysics 51, 453 (2022); https://doi.org/10.1146/annurev-biophys-100521-103031
/content/journals/10.1146/annurev-biophys-100521-103031
/content/journals/10.1146/annurev-biophys-100521-103031
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