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The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase.

Publication ,  Journal Article
Kramer, SP; Johnson, JL; Ribeiro, AA; Millington, DS; Rajagopalan, KV
Published in: J Biol Chem
December 5, 1987

A di-(carboxamidomethyl) derivative of molybdopterin, the organic component of the molybdenum cofactor, has been prepared under conditions favoring retention of all of the structural features of the molecule. The specific radioactivity of [1-14C]iodoacetamide incorporated relative to the amount of phosphate indicated two alkylation sites per pterin. Energy-dispersive x-ray analysis of the derivative showed the presence of 2 sulfurs in the derivative. An exact mass corresponding to the molecular formula C14H18N7O5S2 was obtained for the MH+ ion of the alkylated, dephosphorylated compound by fast atom bombardment mass spectroscopy. 1H NMR spectra of the phosphorylated and dephosphorylated forms of alkylated molybdopterin, in conjunction with the other data, have provided strong corroboration of the validity of the proposed structure of molybdopterin (Johnson, J. L., and Rajagopalan, K. V. (1982) Proc. Natl. Acad. Sci. U. S. A. 79, 6856-6860) as a 6-alkylpterin with a 4-carbon side chain containing an enedithiol on C-1' and C-2', a secondary alcohol on C-3', and a phosphorylated primary alcohol on C-4'. As isolated, the di-(carboxamido-methyl)molybdopterin was found to be a 5,6,7,8-tetrahydropterin.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

December 5, 1987

Volume

262

Issue

34

Start / End Page

16357 / 16363

Location

United States

Related Subject Headings

  • Xanthine Oxidase
  • Pterins
  • Pteridines
  • Oxidoreductases Acting on Sulfur Group Donors
  • Oxidoreductases
  • Molybdenum Cofactors
  • Molybdenum
  • Milk
  • Metalloproteins
  • Mass Spectrometry
 

Citation

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MLA
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Kramer, S. P., Johnson, J. L., Ribeiro, A. A., Millington, D. S., & Rajagopalan, K. V. (1987). The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase. J Biol Chem, 262(34), 16357–16363.
Kramer, S. P., J. L. Johnson, A. A. Ribeiro, D. S. Millington, and K. V. Rajagopalan. “The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase.J Biol Chem 262, no. 34 (December 5, 1987): 16357–63.
Kramer SP, Johnson JL, Ribeiro AA, Millington DS, Rajagopalan KV. The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase. J Biol Chem. 1987 Dec 5;262(34):16357–63.
Kramer SP, Johnson JL, Ribeiro AA, Millington DS, Rajagopalan KV. The structure of the molybdenum cofactor. Characterization of di-(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase. J Biol Chem. 1987 Dec 5;262(34):16357–16363.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

December 5, 1987

Volume

262

Issue

34

Start / End Page

16357 / 16363

Location

United States

Related Subject Headings

  • Xanthine Oxidase
  • Pterins
  • Pteridines
  • Oxidoreductases Acting on Sulfur Group Donors
  • Oxidoreductases
  • Molybdenum Cofactors
  • Molybdenum
  • Milk
  • Metalloproteins
  • Mass Spectrometry