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Structure and Reactivity of the Metal Centers of Ribonucleotide Reductases
Author(s) -
Mulliez Etienne,
Fontecave Marc
Publication year - 1997
Publication title -
chemische berichte
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 0009-2940
DOI - 10.1002/cber.19971300303
Subject(s) - chemistry , ribonucleotide , ribonucleotide reductase , reactivity (psychology) , stereochemistry , enzyme , methionine , sulfur , iron–sulfur cluster , metal , biochemistry , organic chemistry , amino acid , nucleotide , medicine , alternative medicine , pathology , protein subunit , gene
The activation of the three classes of ribonucleotide reductases as free radical enzymes is reviewed. Class I uses O 2 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 O 2 ‐sensitive protein glycyl radical by the concerted action of an iron–sulfur cluster and (S)‐adensoyl methionine.