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

  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},
  volume={230 1},

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.

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.

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.



Characterization of molybdenum cofactor from Escherichia coli

Molybdenum cofactor activity was found in the soluble fraction of cell-free extracts of Escherichia coli grown aerobically in media supplemented with molybdate. Cofactor was detected by its ability

Further purification and properties of Neurospora nitrate reductase.

Purification and properties of the Neurospora crassa assimilatory nitrite reductase.

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