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The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.

Publication ,  Journal Article
Johnson, JL; Hainline, BE; Rajagopalan, KV; Arison, BH
Published in: J Biol Chem
May 10, 1984

Two stable fluorescent derivatives of molybdopterin have been structurally characterized. Form A is an oxidized pterin with a 6-alkyl substituent. Results of chemical, mass spectral, and NMR studies are consistent with the side chain formulation -C identical to C--CH-OHCH2OPO2-3. Similar studies on the Form B derivative indicate that it is the phosphorylated analog of urothione but lacks the 3-methylthio function. Form B (dephospho) can be synthesized from urothione by desulfuration with Raney nickel and oxidation with SeO2. Chicken liver sulfite oxidase (sulfite:ferricytochrome c oxidoreductase, EC 1.8.2.1) contains one phosphate residue (as molybdopterin) per subunit. The phosphate is noncovalently bound but is not released by trichloroacetic acid at 4 degrees C. The yield of Form A and Form B from sulfite oxidase is 0.50 and 0.27/subunit, respectively. The phosphate ester bond in isolated molybdopterin (Form B) is partially hydrolyzed by 1 N HCl at 100 degrees C (33% in 1 h). The release of inorganic phosphate from sulfite oxidase was more rapid (35% in 10 min) due to the presence of molybdate in the denatured enzyme mixture but slower than expected from a high energy phosphate bond. The presence of molybdopterin in a wide variety of molybdenum- and tungsten-containing enzymes has been demonstrated. Glucose oxidase and the iron and manganese superoxide dismutases are devoid of molybdopterin.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

May 10, 1984

Volume

259

Issue

9

Start / End Page

5414 / 5422

Location

United States

Related Subject Headings

  • Xanthine Oxidase
  • Spectrophotometry
  • Spectrometry, Fluorescence
  • Rats
  • Pteridines
  • Oxidoreductases Acting on Sulfur Group Donors
  • Molybdenum Cofactors
  • Molybdenum
  • Metalloproteins
  • Mass Spectrometry
 

Citation

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Johnson, J. L., Hainline, B. E., Rajagopalan, K. V., & Arison, B. H. (1984). The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J Biol Chem, 259(9), 5414–5422.
Johnson, J. L., B. E. Hainline, K. V. Rajagopalan, and B. H. Arison. “The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.J Biol Chem 259, no. 9 (May 10, 1984): 5414–22.
Johnson JL, Hainline BE, Rajagopalan KV, Arison BH. The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J Biol Chem. 1984 May 10;259(9):5414–22.
Johnson, J. L., et al. “The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives.J Biol Chem, vol. 259, no. 9, May 1984, pp. 5414–22.
Johnson JL, Hainline BE, Rajagopalan KV, Arison BH. The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J Biol Chem. 1984 May 10;259(9):5414–5422.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

May 10, 1984

Volume

259

Issue

9

Start / End Page

5414 / 5422

Location

United States

Related Subject Headings

  • Xanthine Oxidase
  • Spectrophotometry
  • Spectrometry, Fluorescence
  • Rats
  • Pteridines
  • Oxidoreductases Acting on Sulfur Group Donors
  • Molybdenum Cofactors
  • Molybdenum
  • Metalloproteins
  • Mass Spectrometry