Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex | Zendy

Gyunghoon Kang | Zendy; Alexander T. Taguchi | Zendy; JoAnne Stubbe | Zendy; Catherine L. Drennan | Zendy

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Structure of a trapped radical transfer pathway within a ribonucleotide reductase holocomplex

Author(s) -

Gyunghoon Kang,

Alexander T. Taguchi,

JoAnne Stubbe,

Catherine L. Drennan

Publication year - 2020

Publication title -

science

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 12.556

H-Index - 1186

eISSN - 1095-9203

pISSN - 0036-8075

DOI - 10.1126/science.aba6794

Subject(s) - ribonucleotide reductase , electron transfer , proton coupled electron transfer , angstrom , chemistry , proton , electron transport chain , electron , biophysics , crystallography , protein subunit , photochemistry , biochemistry , biology , physics , quantum mechanics , gene

Caught in the act Proton-coupled electron transfer (PCET) is an important process for moving electrons through proteins and requires precise positioning of suitable proton and electron carriers. Kanget al. determined a cryo–electron microscopy structure of the active complex formed by ribonucleotide reductase that allows for PCET between two protein subunits over a total distance of ∼35 angstroms. Several interventions that stabilized the radical en route also stabilized the complex and allowed for visualization of the interface between the two subunits and the full network of residues that permit PCET.Science , this issue p.424

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