ArticleThe Journal of biological chemistry2013
Identification of a bis-molybdopterin intermediate in molybdenum cofactor biosynthesis in Escherichia coli.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 48 citations in OpenAlex.
- Transformation of tetranuclear [{MoOChemical communications (Cambridge, England) · 2026Article
- Operando photocatalytic cell for time-resolved XAS/GC analysis of gas phase COJournal of synchrotron radiation · 2026Article
- Iron limitation indirectly reduces theMicrobiology spectrum · 2024Article
- A step into the rare biosphere: genomic features of the new genusFrontiers in microbiology · 2023Article
- The Role of the Nucleotides in the Insertion of the bis-Molybdopterin Guanine Dinucleotide Cofactor into apo-Molybdoenzymes.Molecules (Basel, Switzerland) · 2022Article
- Salicylate coordination in metal-protochelin complexes.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2022Article
- Fabrication and characterisation of a silicon-borosilicate glass microfluidic device for synchrotron-based hard X-ray spectroscopy studies.RSC advances · 2021Article
- Iron-Dependent Regulation of Molybdenum Cofactor Biosynthesis Genes in Escherichia coli.Journal of bacteriology · 2019Article
- DMSO Reductase Family: Phylogenetics and Applications of Extremophiles.International journal of molecular sciences · 2019Review
- Molybdenum cofactor transfer from bacteria to nematode mediates sulfite detoxification.Nature chemical biology · 2019Article
- Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.PloS one · 2018Article
- Transcriptional regulation of dimethyl sulfoxide respiration in a haloarchaeon, Haloferax volcanii.Extremophiles : life under extreme conditions · 2016Article
- Structural Basis for Oxygen Activation at a Heterodinuclear Manganese/Iron Cofactor.The Journal of biological chemistry · 2015Article
- The role of FeS clusters for molybdenum cofactor biosynthesis and molybdoenzymes in bacteria.Biochimica et biophysica acta · 2015Review
- The biosynthesis of the molybdenum cofactors.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015Article
- bis-Molybdopterin guanine dinucleotide is required for persistence of Mycobacterium tuberculosis in guinea pigs.Infection and immunity · 2015Article
- Bacterial formate hydrogenlyase complex.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- The mononuclear molybdenum enzymes.Chemical reviews · 2014Review
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Authors and funding
9 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The molybdenum cofactor is an important cofactor, and its biosynthesis is essential for many organisms, including humans. Its basic form comprises a single molybdopterin (MPT) unit, which binds a molybdenum ion bearing three oxygen ligands via a dithiolene function, thus forming Mo-MPT. In bacteria, this form is modified to form the bis-MPT guanine dinucleotide cofactor with two MPT units coordinated at one molybdenum atom, which additionally contains GMPs bound to the terminal phosphate group of the MPTs (bis-MGD). The MobA protein catalyzes the nucleotide addition to MPT, but the mechanism of the biosynthesis of the bis-MGD cofactor has remained enigmatic. We have established an in vitro system for studying bis-MGD assembly using purified compounds. Quantification of the MPT/molybdenum and molybdenum/phosphorus ratios, time-dependent assays for MPT and MGD detection, and determination of the numbers and lengths of Mo-S and Mo-O bonds by X-ray absorption spectroscopy enabled identification of a novel bis-Mo-MPT intermediate on MobA prior to nucleotide attachment. The addition of Mg-GTP to MobA loaded with bis-Mo-MPT resulted in formation and release of the final bis-MGD product. This cofactor was fully functional and reconstituted the catalytic activity of apo-TMAO reductase (TorA). We propose a reaction sequence for bis-MGD formation, which involves 1) the formation of bis-Mo-MPT, 2) the addition of two GMP units to form bis-MGD on MobA, and 3) the release and transfer of the mature cofactor to the target protein TorA, in a reaction that is supported by the specific chaperone TorD, resulting in an active molybdoenzyme.
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