ArticleBiochemistry research international2011
The role of system-specific molecular chaperones in the maturation of molybdoenzymes in bacteria.
Article in Biochemistry research international, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 35 citations in OpenAlex.
- One Hundred Years of Sulfido Ligand in the Molybdenum Cofactor: New Perspectives.Chembiochem : a European journal of chemical biology · 2026Review
- The presence and induction of regioselective dehydroxylases dictate urolithin metabolism by Enterocloster species.NPJ biofilms and microbiomes · 2025Article
- Evolution of two metabolic genes involved in nucleotide and amino acid metabolism in Pseudomonas aeruginosa.PloS one · 2024Article
- A putative xanthine dehydrogenase is critical forMicrobiology (Reading, England) · 2023Article
- Same but different: Comparison of two system-specific molecular chaperones for the maturation of formate dehydrogenases.PloS one · 2018Article
- Chaperones in maturation of molybdoenzymes: Why specific is better than general?Bioengineered · 2017Article
- Discovery of piperonal-converting oxidase involved in the metabolism of a botanical aromatic aldehyde.Scientific reports · 2016Article
- 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
- Insights into the posttranslational assembly of the Mo-, S- and Cu-containing cluster in the active site of CO dehydrogenase of Oligotropha carboxidovorans.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014Article
- Structural data on the periplasmic aldehyde oxidoreductase PaoABC from Escherichia coli: SAXS and preliminary X-ray crystallography analysis.International journal of molecular sciences · 2014Article
- Biochemical, stabilization and crystallization studies on a molecular chaperone (PaoD) involved in the maturation of molybdoenzymes.PloS one · 2014Article
- Identification of a bis-molybdopterin intermediate in molybdenum cofactor biosynthesis in Escherichia coli.The Journal of biological chemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biogenesis of prokaryotic molybdoenzymes is a complex process with the final step representing the insertion of a matured molybdenum cofactor (Moco) into a folded apoenzyme. Usually, specific chaperones of the XdhC family are required for the maturation of molybdoenzymes of the xanthine oxidase family in bacteria. Enzymes of the xanthine oxidase family are characterized to contain an equatorial sulfur ligand at the molybdenum center of Moco. This sulfur ligand is inserted into Moco while bound to the XdhC-like protein and before its insertion into the target enzyme. In addition, enzymes of the xanthine oxidase family bind either the molybdopterin (Mo-MPT) form of Moco or the modified molybdopterin cytosine dinucleotide cofactor (MCD). In both cases, only the matured cofactor is inserted by a proofreading process of XdhC. The roles of these specific XdhC-like chaperones during the biogenesis of enzymes of the xanthine oxidase family in bacteria are described.
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