期刊
ANNUAL REVIEW OF BIOCHEMISTRY, VOL 80
卷 80, 期 -, 页码 733-767出版社
ANNUAL REVIEWS
DOI: 10.1146/annurev-biochem-061408-095817
关键词
accessory factors/proteins; cofactor maturation; iron and manganese homeostasis; metal specificity; posttranslational modification; protein radicals
资金
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R37GM029595, R01GM029595, R01GM081393] Funding Source: NIH RePORTER
- NIGMS NIH HHS [R01 GM081393, GM29595, R01 GM029595, GM81393] Funding Source: Medline
Incorporation of metallocofactors essential for the activity of many enyzmes is a major mechanism of posttranslational modification. The cellular machinery required for these processes in the case of mono- and dinuclear nonheme iron and manganese cofactors has remained largely elusive. In addition, many metallocofactors can be converted to inactive forms, and pathways for their repair have recently come to light. The class I ribonucleotide reductases (RNRs) catalyze the conversion of nucleotides to deoxynucleotides and require dinuclear metal clusters for activity: an (FeFeIII)-Fe-III-tyrosyl radical (Y center dot) cofactor (class la), a (MnMnIII)-Mn-III-Y center dot cofactor (class Ib), and a (MnFeIII)-Fe-IV cofactor (class Ic). The class Ia, Ib, and Ic RNRs are structurally homologous and contain almost identical metal coordination sites. Recent progress in our understanding of the mechanisms by which the cofactor of each of these RNRs is generated in vitro and in vivo and by which the damaged cofactors are repaired is providing insight into how nature prevents mismetallation and orchestrates active cluster formation in high yields.
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