ArticleThe Journal of biological chemistry2017
A unique cysteine-rich zinc finger domain present in a majority of class II ribonucleotide reductases mediates catalytic turnover.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Ribonucleotide reductases recapitulate biogeographic patterns within virioplankton according to ocean biogeochemistry.bioRxiv : the preprint server for biology · 2026Article
- Real-time assay of ribonucleotide reductase activity with a fluorescent RNA aptamer.FEBS letters · 2026Article
- Chymotrypsin digestion analysis of glycyl radical and B12-dependent radical enzymes indicates common substrate-induced structural shifts.Scientific reports · 2025Article
- Foam fractionation Tags (F-Tags) enabling surfactant-free, activity-preserving recovery of enzymes.Applied microbiology and biotechnology · 2024Article
- Analysis of insertions and extensions in the functional evolution of the ribonucleotide reductase family.Protein science : a publication of the Protein Society · 2022Article
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- Biotechnological and Biomedical Applications of Enzymes Involved in the Synthesis of Nucleosides and Nucleotides.Biomolecules · 2021Article
- Structural determinants and distribution of phosphate specificity in ribonucleotide reductases.The Journal of biological chemistry · 2021Article
- Article
- Non-host class II ribonucleotide reductase in Thermus viruses: sequence adaptation and host interaction.PeerJ · 2019Article
- Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ribonucleotide reductases (RNRs) catalyze the reduction of ribonucleotides to the corresponding deoxyribonucleotides, used in DNA synthesis and repair. Two different mechanisms help deliver the required electrons to the RNR active site. Formate can be used as reductant directly in the active site, or glutaredoxins or thioredoxins reduce a C-terminal cysteine pair, which then delivers the electrons to the active site. Here, we characterized a novel cysteine-rich C-terminal domain (CRD), which is present in most class II RNRs found in microbes. The NrdJd-type RNR from the bacterium
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