ArticleThe Journal of biological chemistry2011
NrdH-redoxin protein mediates high enzyme activity in manganese-reconstituted ribonucleotide reductase from Bacillus anthracis.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 35 citations in OpenAlex.
- Unveiling the probiotic potential of the genus Geobacillus through comparative genomics and in silico analysis.Scientific reports · 2025Article
- Optimizing Divalent Cation Supplementation to Enhance the Production of the Kimchi Starter StrainJournal of microbiology and biotechnology · 2025Article
- Thioredoxin reductase from Bacillus cereus exhibits distinct reduction and NADPH-binding properties.FEBS open bio · 2021Article
- Convergent allostery in ribonucleotide reductase.Nature communications · 2019Article
- Genomic characterization of three novel Basilisk-like phages infecting Bacillus anthracis.BMC genomics · 2018Article
- An endogenous dAMP ligand inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Ribonucleotide Reductases from Bifidobacteria Contain Multiple Conserved Indels Distinguishing Them from All Other Organisms:Frontiers in microbiology · 2017Article
- Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.The Journal of biological chemistry · 2015Article
- Methyl-hydroxylamine as an efficacious antibacterial agent that targets the ribonucleotide reductase enzyme.PloS one · 2015Article
- Semiquinone-induced maturation of Bacillus anthracis ribonucleotide reductase by a superoxide intermediate.The Journal of biological chemistry · 2014Article
- Choosing the right metal: case studies of class I ribonucleotide reductases.The Journal of biological chemistry · 2014Review
- Assembly of nonheme Mn/Fe active sites in heterodinuclear metalloproteins.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Review
- The class Ib ribonucleotide reductase from Mycobacterium tuberculosis has two active R2F subunits.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Phosphines are ribonucleotide reductase reductants that act via C-terminal cysteines similar to thioredoxins and glutaredoxins.Scientific reports · 2014Article
- Streptococcus sanguinis class Ib ribonucleotide reductase: high activity with both iron and manganese cofactors and structural insights.The Journal of biological chemistry · 2014Article
- Genetic characterization and role in virulence of the ribonucleotide reductases of Streptococcus sanguinis.The Journal of biological chemistry · 2014Article
- Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.Biochemistry · 2014Article
- Ribonucleotide reductases: essential enzymes for bacterial life.Frontiers in cellular and infection microbiology · 2014Review
- Mechanism of assembly of the dimanganese-tyrosyl radical cofactor of class Ib ribonucleotide reductase: enzymatic generation of superoxide is required for tyrosine oxidation via a Mn(III)Mn(IV) intermediate.Journal of the American Chemical Society · 2013Article
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Authors and funding
9 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacillus anthracis is a severe mammalian pathogen encoding a class Ib ribonucleotide reductase (RNR). RNR is a universal enzyme that provides the four essential deoxyribonucleotides needed for DNA replication and repair. Almost all Bacillus spp. encode both class Ib and class III RNR operons, but the B. anthracis class III operon was reported to encode a pseudogene, and conceivably class Ib RNR is necessary for spore germination and proliferation of B. anthracis upon infection. The class Ib RNR operon in B. anthracis encodes genes for the catalytic NrdE protein, the tyrosyl radical metalloprotein NrdF, and the flavodoxin protein NrdI. The tyrosyl radical in NrdF is stabilized by an adjacent Mn(2)(III) site (Mn-NrdF) formed by the action of the NrdI protein or by a Fe(2)(III) site (Fe-NrdF) formed spontaneously from Fe(2+) and O(2). In this study, we show that the properties of B. anthracis Mn-NrdF and Fe-NrdF are in general similar for interaction with NrdE and NrdI. Intriguingly, the enzyme activity of Mn-NrdF was approximately an order of magnitude higher than that of Fe-NrdF in the presence of the class Ib-specific physiological reductant NrdH, strongly suggesting that the Mn-NrdF form is important in the life cycle of B. anthracis. Whether the Fe-NrdF form only exists in vitro or whether the NrdF protein in B. anthracis is a true cambialistic enzyme that can work with either manganese or iron remains to be established.
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