The pterin of the molybdenum cofactor.

Journal Article (Journal Article)

The molybdenum cofactor common to a variety of molybdoenzymes has been shown to contain a novel pterin. The pterin has been isolated from sulfite oxidase from several sources, xanthine-oxidizing enzymes from milk and chicken liver, and nitrate reductase of Chlorella vulgaris after denaturation of the proteins in the presence of I2. Investigation of the anionic nature of the isolated pterin has revealed that it is a monophosphate ester susceptible to cleavage by alkaline phosphatase. Quantitative analyses have shown that one molecule of the pterin phosphate is associated with each molybdenum atom in sulfite oxidase. Studies to date have shown that the pterin is present in a reduced form in sulfite oxidase and xanthine dehydrogenase, and that in situ oxidation of the pterin leads to inactivation of sulfite oxidase.

Full Text

Duke Authors

Cited Authors

  • Rajagopalan, KV; Johnson, JL; Hainline, BE

Published Date

  • July 1982

Published In

Volume / Issue

  • 41 / 9

Start / End Page

  • 2608 - 2612

PubMed ID

  • 6953016

International Standard Serial Number (ISSN)

  • 0014-9446


  • eng

Conference Location

  • United States