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Structure and Reactivity of the Metal Centers of Ribonucleotide Reductases (1997)

Mulliez, Etienne ; Fontecave, Marc

Weinheim : Wiley-Blackwell

Berichte der deutschen chemischen Gesellschaft 130 (1997), S. 317-322

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ISSN: 0009-2940

Keywords: Ribonucleotide reductase ; Tyrosyl radical ; Adenosyl radical ; Glycyl radical ; Iron-sulfur cluster ; Cobalamin ; (S)-Adenosyl methionine ; Chemistry ; Inorganic Chemistry

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Chemistry and Pharmacology

Notes: The 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.

Additional Material: 1 Ill.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1002/cber.19971300303

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