The relationship of Mo, molybdopterin, and the cyanolyzable sulfur in the Mo cofactor.

@article{Wahl1984TheRO,
  title={The relationship of Mo, molybdopterin, and the cyanolyzable sulfur in the Mo cofactor.},
  author={Rosemarie Wahl and Robert V. Hageman and Krishnan Rajagopalan},
  journal={Archives of biochemistry and biophysics},
  year={1984},
  volume={230 1},
  pages={
          264-73
        }
}
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41 Citations

Studies on the oxidation state of molybdopterin

Molybdenum cofactor biosynthesis and molybdenum enzymes.

The molybdenum cofactor (Moco) forms the active site of all eukaryotic moly bdenum (Mo) enzymes and is essential for purine degradation and stress response.

In vitro reconstitution of nitrate reductase activity of the Neurospora crassa mutant nit-1: specific incorporation of molybdopterin.

Regulation of molybdenum cofactor species in the green alga Chlamydomonas reinhardtii.

Molybdenum cofactor biosynthesis and deficiency

  • G. Schwarz
  • Chemistry, Biology
    Cellular and Molecular Life Sciences CMLS
  • 2005
Human Moco deficiency is a hereditary metabolic disorder characterized by severe neurodegeneration resulting inEarly childhood death resulting in early childhood death and a first substitution therapy was established.

The Chlamydomonas reinhardtii MoCo carrier protein is multimeric and stabilizes molybdopterin cofactor in a molybdate charged form

Purification and characterization of the molybdoenzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini

The enzymes nicotinate dehydrogenase and 6-hydroxynicotinate dehydrogenase from Bacillus niacini could be purified to homogeneity by means of anion exchange chromatography, hydrophobic interaction…

The pterin (bactopterin) of carbon monoxide dehydrogenase from Pseudomonas carboxydoflava.

Radioactively labeled carbon monoxide (CO) dehydrogenase has been obtained in good yield and purity from Pseudomonas carboxydoflava grown in the presence of [32P]phosphate, and contained a novel pterin, different from molybdopterin, which was tentatively named bactopterin.

Rhodobacter capsulatus XdhC Is Involved in Molybdenum Cofactor Binding and Insertion into Xanthine Dehydrogenase*

It is shown that XdhC is required for the stabilization of the sulfurated form of Moco present in enzymes of the xanthine oxidase family, implying that enzyme-specific proteins exist for the biogenesis of molybdoenzymes, coordinating Moco binding and insertion into their respective target proteins.

[62] Assay and detection of the molybdenum cofactor

References

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Involvement of molybdenum and iron in the in vitro assembly of assimilatory nitrate reductase utilizing Neurospora mutant nit-1.

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The enzyme activities are inhibited on preincubation with either reduced pyridine nucleotide electron donor (NADPH or NADH), provided FAD is present, and the electron acceptors, nitrite and hydroxylamine, protect against this inactivation.

Characterization of the molybdenum cofactor of sulfite oxidase, xanthine, oxidase, and nitrate reductase. Identification of a pteridine as a structural component.

The molybdenum cofactor has been isolated in an oxidized inactive form from purified molybdoenzymes. The isolated material is shown to be a novel pterin. The active cofactor is presumably composed of…

Drosophila melanogaster ma-l mutants are defective in the sulfuration of desulfo Mo hydroxylases.

Molecular basis of the biological function of molybdenum. Effect of tungsten on xanthine oxidase and sulfite oxidase in the rat.