Structure and Reactivity of the Metal Centers of Ribonucleotide Reductases

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AbstractThe activation of the three classes of ribonucleotide reductases as free radical enzymes is reviewed. Class I uses O2 and a diferric μ‐oxo center to generate a stable tyrosyl protein radical. Class II operates with adensoyl cobalamin as the precursor of a putative transient thiyl protein glycyl radical by the concerted forms an O2‐sensitive protein glycyl radical by the concerted action of an iron–sulfur cluster and (S)‐adensoyl methionine.