Control of metallation and active cofactor assembly in the class Ia and Ib ribonucleotide reductases: diiron or dimanganese?
Name
Stubbe_Control of.pdf
Size
1.25 MB
Format
Adobe PDF
Checksum (MD5)
5994cda806695fdfc3a6af216f0ae925
Author(s)
Stubbe, JoAnne
Cotruvo, Joseph A.
Date Issued
January 2011
Journal
Current Opinion in Chemical Biology
Publisher
Elsevier
Citation
Stubbe, JoAnne, and Joseph A Cotruvo. “Control of Metallation and Active Cofactor Assembly in the Class Ia and Ib Ribonucleotide Reductases: Diiron or Dimanganese?” Current Opinion in Chemical Biology 15, no. 2 (April 2011): 284–90.
Version
Author's final manuscript
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 O[subscript 2] 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 Mn[superscript II] and Fe[superscript II], 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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-NoDerivatives
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1016/j.cbpa.2010.12.001
