Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: Diiron or dimanganese?

Jo Anne Stubbe, Joseph A. Cotruvo

Research output: Contribution to journalReview articlepeer-review

17 Scopus citations

Abstract

Ribonucleotide reductases (RNRs) convert nucleotides to deoxynucleotides in all organisms. Activity of the class Ia and Ib RNRs requires a stable tyrosyl radical (Y), which can be generated by the reaction of O2 with a diferrous cluster on the β subunit to form active diferric-Y cofactor. Recent experiments have demonstrated, however, that in vivo the class Ib RNR contains an active dimanganese(III)-Y cofactor. The similar metal binding sites of the class Ia and Ib RNRs, their ability to bind both MnII and FeII, and the activity of the class Ib RNR with both diferric-Y and dimanganese(III)-Y cofactors raise the intriguing question of how the cell prevents mismetallation of these essential enzymes. The presence of the class Ib RNR in numerous pathogenic bacteria also highlights the importance of manganese for these organisms' growth and virulence.

Original languageEnglish (US)
Pages (from-to)284-290
Number of pages7
JournalCurrent Opinion in Chemical Biology
Volume15
Issue number2
DOIs
StatePublished - Apr 2011

All Science Journal Classification (ASJC) codes

  • Analytical Chemistry
  • Biochemistry

Fingerprint Dive into the research topics of 'Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: Diiron or dimanganese?'. Together they form a unique fingerprint.

Cite this