The prototypic class Ia ribonucleotide reductase from Escherichia coli: still surprising after all these years
Name
Manuscript_Drennan_2012March13with figures.pdf
Size
5.05 MB
Format
Adobe PDF
Checksum (MD5)
54d2b413c7e57538585a742ab728749a
Author(s)
Ando, Nozomi
Zimanyi, Christina Marie
Brignole, Edward J
Drennan, Catherine L
Date Issued
June 2012
Journal
Biochemical Society Transactions
Publisher
Portland Press
Citation
Brignole, Edward J. et al. “The Prototypic Class Ia Ribonucleotide Reductase from Escherichia Coli: Still Surprising After All These Years.” Biochemical Society Transactions 40.3 (2012): 523–530. Web.
Version
Author's final manuscript
Abstract
RNRs (ribonucleotide reductases) are key players in nucleic acid metabolism, converting ribonucleotides into deoxyribonucleotides. As such, they maintain the intracellular balance of deoxyribonucleotides to ensure the fidelity of DNA replication and repair. The best-studied RNR is the class Ia enzyme from Escherichia coli, which employs two subunits to catalyse its radical-based reaction: β2 houses the diferric-tyrosyl radical cofactor, and α2 contains the active site. Recent applications of biophysical methods to the study of this RNR have revealed the importance of oligomeric state to overall enzyme activity and suggest that unprecedented subunit configurations are in play. Although it has been five decades since the isolation of nucleotide reductase activity in extracts of E. coli, this prototypical RNR continues to surprise us after all these years.
MIT Department
Massachusetts Institute of Technology. Department of Biology
Massachusetts Institute of Technology. Department of Chemistry
Terms of Use
Creative Commons Attribution-Noncommercial-Share Alike 3.0
Persistent DSpace Link
DOI of Published Version
https://doi.org/10.1042/BST20120081
