Conformationally gated multisite proton-coupled electron transfer in the ribonucleotide reductase <i>β</i> subunit.

ABSTRACT: Ribonucleotide reductase (RNR) is an essential enzyme that converts ribonucleotides into deoxyribonucleotides, enabling DNA synthesis and repair in all living organisms. Central to class Ia RNR activity is a long-range radical transport pathway spanning [Formula: see text]32 Å across the [Formula: see text] and [Formula: see text] subunits by a series of proton-coupled electron transfer (PCET) reactions. Although the collinear PCET reactions in the [Formula: see text] subunit have been extensively studied, the multisite, orthogonal PCET reactions in the [Formula: see text] subunit are less well understood. This work focuses on orthogonal PCET between the redox-active tryptophan, W48, and interfacial tyrosine, Y356, in the [Formula: see text] subunit. Multiscale modeling strategies are empl

SUBMITTER: Deng J 

PROVIDER: S-EPMC12867644 | biostudies-literature | 2026 Feb

REPOSITORIES: biostudies-literature