ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2014
The class Ib ribonucleotide reductase from Mycobacterium tuberculosis has two active R2F subunits.
Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Characterization of a second class Ie ribonucleotide reductase.Communications biology · 2025Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Subunit Interaction Dynamics of Class Ia Ribonucleotide Reductases: In Search of a Robust Assay.Biochemistry · 2020Article
- Harnessing Biological Insight to Accelerate Tuberculosis Drug Discovery.Accounts of chemical research · 2019Review
- DNA Replication in Mycobacterium tuberculosis.Microbiology spectrum · 2017Review
- Methyl-hydroxylamine as an efficacious antibacterial agent that targets the ribonucleotide reductase enzyme.PloS one · 2015Article
- Phylogenetic analysis of vitamin B12-related metabolism in Mycobacterium tuberculosis.Frontiers in molecular biosciences · 2015Review
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Authors and funding
6 authors.
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Abstract
Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to their corresponding deoxyribonucleotides, playing a crucial role in DNA repair and replication in all living organisms. Class Ib RNRs require either a diiron-tyrosyl radical (Y·) or a dimanganese-Y· cofactor in their R2F subunit to initiate ribonucleotide reduction in the R1 subunit. Mycobacterium tuberculosis, the causative agent of tuberculosis, contains two genes, nrdF1 and nrdF2, encoding the small subunits R2F-1 and R2F-2, respectively, where the latter has been thought to serve as the only active small subunit in the M. tuberculosis class Ib RNR. Here, we present evidence for the presence of an active Fe 2 (III) -Y· cofactor in the M. tuberculosis RNR R2F-1 small subunit, supported and characterized by UV-vis, X-band electron paramagnetic resonance, and resonance Raman spectroscopy, showing features similar to those for the M. tuberculosis R2F-2-Fe 2 (III) -Y· cofactor. We also report enzymatic activity of Fe 2 (III) -R2F-1 when assayed with R1, and suggest that the active M. tuberculosis class Ib RNR can use two different small subunits, R2F-1 and R2F-2, with similar activity.
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