ArticleBiochemistry2011
Bacillus subtilis class Ib ribonucleotide reductase is a dimanganese(III)-tyrosyl radical enzyme.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Kinetically Divergent Dimanganese-Tyrosyl Radical Cofactor Assembly in Listeria monocytogenes Class I Ribonucleotide Reductase.Biochemistry · 2026Article
- A Structurally Divergent Class Ia Ribonucleotide Reductase from a Tick-Borne Pathogen.Biochemistry · 2025Article
- Genome sequence of the plant-growth-promoting bacterium Bacillus velezensis EU07.Access microbiology · 2024Article
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.Journal of the American Chemical Society · 2023Article
- Enzymatic Hydroxylation of Aliphatic C-H Bonds by a Mn/Fe Cofactor.bioRxiv : the preprint server for biology · 2023Article
- Why is manganese so valuable to bacterial pathogens?Frontiers in cellular and infection microbiology · 2023Review
- Hydroxyurea Induces a Stress Response That Alters DNA Replication and Nucleotide Metabolism in Bacillus subtilis.Journal of bacteriology · 2021Article
- Article
- The Bacillus anthracis class Ib ribonucleotide reductase subunit NrdF intrinsically selects manganese over iron.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Article
- Chemical flexibility of heterobimetallic Mn/Fe cofactors: R2lox and R2c proteins.The Journal of biological chemistry · 2019Article
- Redox-induced structural changes in the di-iron and di-manganese forms of Bacillus anthracis ribonucleotide reductase subunit NrdF suggest a mechanism for gating of radical access.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Convergent allostery in ribonucleotide reductase.Nature communications · 2019Article
- Assembly of a heterodinuclear Mn/Fe cofactor is coupled to tyrosine-valine ether cross-link formation in the R2-like ligand-binding oxidase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2019Article
- Ether cross-link formation in the R2-like ligand-binding oxidase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- An endogenous dAMP ligand inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Involvement of high-valent manganese-oxo intermediates in oxidation reactions: realisation in nature, nano and molecular systems.Nano convergence · 2018Review
- Role of Ribonucleotide Reductase in Bacillus subtilis Stress-Associated Mutagenesis.Journal of bacteriology · 2017Article
- Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.The Journal of biological chemistry · 2015Article
- Manganese homeostasis and utilization in pathogenic bacteria.Molecular microbiology · 2015Review
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2 authors.
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Abstract
Bacillus subtilis class Ib ribonucleotide reductase (RNR) catalyzes the conversion of nucleotides to deoxynucleotides, providing the building blocks for DNA replication and repair. It is composed of two proteins: α (NrdE) and β (NrdF). β contains the metallo-cofactor, essential for the initiation of the reduction process. The RNR genes are organized within the nrdI-nrdE-nrdF-ymaB operon. Each protein has been cloned, expressed, and purified from Escherichia coli. As isolated, recombinant NrdF (rNrdF) contained a diferric-tyrosyl radical [Fe(III)(2)-Y(•)] cofactor. Alternatively, this cluster could be self-assembled from apo-rNrdF, Fe(II), and O(2). Apo-rNrdF loaded using 4 Mn(II)/β(2), O(2), and reduced NrdI (a flavodoxin) can form a dimanganese(III)-Y(•) [Mn(III)(2)-Y(•)] cofactor. In the presence of rNrdE, ATP, and CDP, Mn(III)(2)-Y(•) and Fe(III)(2)-Y(•) rNrdF generate dCDP at rates of 132 and 10 nmol min(-1) mg(-1), respectively (both normalized for 1 Y(•)/β(2)). To determine the endogenous cofactor of NrdF in B. subtilis, the entire operon was placed behind a Pspank(hy) promoter and integrated into the B. subtilis genome at the amyE site. All four genes were induced in cells grown in Luria-Bertani medium, with levels of NrdE and NrdF elevated 35-fold relative to that of the wild-type strain. NrdE and NrdF were copurified in a 1:1 ratio from this engineered B. subtilis. The visible, EPR, and atomic absorption spectra of the purified NrdENrdF complex (eNrdF) exhibited characteristics of a Mn(III)(2)-Y(•) center with 2 Mn/β(2) and 0.5 Y(•)/β(2) and an activity of 318-363 nmol min(-1) mg(-1) (normalized for 1 Y(•)/β(2)). These data strongly suggest that the B. subtilis class Ib RNR is a Mn(III)(2)-Y(•) enzyme.
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