ArticleJournal of the American Chemical Society2013
Identification of a cyclic nucleotide as a cryptic intermediate in molybdenum cofactor biosynthesis.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 80 citations in OpenAlex.
- Beyond native reactivity: radical SAM enzymes as platforms for new-to-nature chemistry.RSC chemical biology · 2026Review
- Guiding covalent catalysis enables a carbon-inserting rearrangement in molybdenum cofactor biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Emerging roles of pterins as signaling molecules in bacteria.Biochemical Society transactions · 2026Review
- The Radical SAM Enzyme BlsE Can Operate as a Dehydratase, Dehydrogenase, or Epimerase upon Mutation of a Single Active Site Serine Residue.Journal of the American Chemical Society · 2026Article
- Mechanism of controlled radical initiation in radical SAM GTP 3',8-cyclase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Iron limitation indirectly reduces theMicrobiology spectrum · 2024Article
- The structural principles underlying molybdenum insertase complex assembly.Protein science : a publication of the Protein Society · 2023Article
- Moco Carrier and Binding Proteins.Molecules (Basel, Switzerland) · 2022Review
- Function of Molybdenum Insertases.Molecules (Basel, Switzerland) · 2022Review
- Resolving the Multidecade-Long Mystery in MoaA Radical SAM Enzyme Reveals New Opportunities to Tackle Human Health Problems.ACS bio & med chem Au · 2022Review
- Characterizing SPASM/twitch Domain-Containing Radical SAM Enzymes by EPR Spectroscopy.Applied magnetic resonance · 2022Review
- HygY Is a Twitch Radical SAM Epimerase with Latent Dehydrogenase Activity Revealed upon Mutation of a Single Cysteine Residue.Journal of the American Chemical Society · 2021Article
- Mechanism of Reduction of an Aminyl Radical Intermediate in the Radical SAM GTP 3',8-Cyclase MoaA.Journal of the American Chemical Society · 2021Article
- Mechanism of molybdate insertion into pterin-based molybdenum cofactors.Nature chemistry · 2021Article
- Dph3 Enables Aerobic Diphthamide Biosynthesis by Donating One Iron Atom to Transform a [3Fe-4S] to a [4Fe-4S] Cluster in Dph1-Dph2.Journal of the American Chemical Society · 2021Article
- Computational Approaches: An Underutilized Tool in the Quest to Elucidate Radical SAM Dynamics.Molecules (Basel, Switzerland) · 2021Review
- Viperin: An ancient radical SAM enzyme finds its place in modern cellular metabolism and innate immunity.The Journal of biological chemistry · 2020Review
- Mechanism of Rate Acceleration of Radical C-C Bond Formation Reaction by a Radical SAM GTP 3',8-Cyclase.Journal of the American Chemical Society · 2020Article
- The First Step ofMicroorganisms · 2020Article
- Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria.Frontiers in microbiology · 2020Review
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The molybdenum cofactor (Moco) is a redox cofactor found in all kingdoms of life, and its biosynthesis is essential for survival of many organisms, including humans. The first step of Moco biosynthesis is a unique transformation of guanosine 5'-triphosphate (GTP) into cyclic pyranopterin monophosphate (cPMP). In bacteria, MoaA and MoaC catalyze this transformation, although the specific functions of these enzymes were not fully understood. Here, we report the first isolation and structural characterization of a product of MoaA. This molecule was isolated under anaerobic conditions from a solution of MoaA incubated with GTP, S-adenosyl-L-methionine, and sodium dithionite in the absence of MoaC. Structural characterization by chemical derivatization, MS, and NMR spectroscopy suggested the structure of this molecule to be (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate (3',8-cH2GTP). The isolated 3',8-cH2GTP was converted to cPMP by MoaC or its human homologue, MOCS1B, with high specificities (Km < 0.060 μM and 0.79 ± 0.24 μM for MoaC and MOCS1B, respectively), suggesting the physiological relevance of 3',8-cH2GTP. These observations, in combination with some mechanistic studies of MoaA, unambiguously demonstrate that MoaA catalyzes a unique radical C-C bond formation reaction and that, in contrast to previous proposals, MoaC plays a major role in the complex rearrangement to generate the pyranopterin ring.
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