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 molybdenum and a reduced form of the pterin.
D000818:Animals; D002645:Chickens; D003067:Coenzymes; D008099:Liver / Q000201:enzymology; D008667:Metalloproteins; D008982:Molybdenum / Q000032:analysis*; D000090006:Molybdenum Cofactors; D009565:Nitrate Reductases; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D011621:Pteridines / Q000032:analysis*; D051381:Rats; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D014969:Xanthine Oxidase
D003067:Coenzymes; D008667:Metalloproteins; D008982:Molybdenum; D000090006:Molybdenum Cofactors; D009565:Nitrate Reductases; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D011621:Pteridines; D014969:Xanthine Oxidase; C022261:molybdopterin