1887

Abstract

Purine hydroxylase I from was purified 850-fold. The purified preparations exhibited the spectral and catalytic properties, including broad specificity for oxidizing and reducing substrates, typical of molybdenum/flavin/iron-sulphur-containing hydroxylases (oxotransferases).

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1989-02-01
2024-04-27
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References

  1. Bell J.M., Colby J., Williams E. 1988; CO oxidoreductase from Streptomyces strain G26 is a molybdenum hydroxylase. Biochemical Journal 250:605–612
    [Google Scholar]
  2. Berg J.M., Holm R.H. 1985a; Model for the active site of oxo-transfer molybdoenzymes: synthesis, structure and properties. Journal of the American Chemical Society 107:917–925
    [Google Scholar]
  3. Berg J.M., Holm R.H. 1985b; Model for the active site of oxo-transfer molybdoenzymes: reactivity, kinetics and catalysis. Journal of the American Chemical Society 107:925–932
    [Google Scholar]
  4. Cleere W.F., Coughlan M.P. 1975; Avian xanthine dehydrogenase. I. Isolation and characterization of the turkey liver enzyme. Comparative Biochemistry and Physiology B50:311–322
    [Google Scholar]
  5. Coughlan M.P. 1980a; Aldehyde oxidase, xanthine oxidase and xanthine dehydrogenase: hydroxylases containing molybdenum, iron-sulphur and flavin. In Molybdenum and Molybdenum-containing Enzymes pp 119–185 Coughlan M. P. Edited by Oxford: Pergamon Press;
    [Google Scholar]
  6. Coughlan M.P. editor 1980b Molybdenum and Molybdenum-containing Enzymes Oxford: Pergamon Press;
    [Google Scholar]
  7. Coughlan M.P. 1983; The role of molybdenum in human biology. Journal of Inherited Metabolic Diseases 6: Suppl.1 70–77
    [Google Scholar]
  8. Coughlan M.P., Mehra R.K., Barber M.J., Siegel L.M. 1984; Optical and electron paramagnetic resonance spectrophotometric studies on purine hydroxylase II from Aspergillus nidulans . Archives of Biochemistry and Biophysics 229:311–316
    [Google Scholar]
  9. Friedrich C.C., Meyer O., Chandra T.S. 1986; Molybdenum-dependent sulphur oxidation in facultatively lithoautotrophic thiobacteria. FEMS Microbiology Letters 37:105–108
    [Google Scholar]
  10. Greenlee L., Handler P. 1964; Xanthine oxidase. VI The influence of pH on substrate specificity. Journal of Biological Chemistry 239:1090–1095
    [Google Scholar]
  11. Hartree E.F. 1972; Determination of protein. A modification of the Lowry method that gives a linear photometric response. Analytical Biochemistry 48:422–427
    [Google Scholar]
  12. Hinojosa-Leon M., Dubourdieu M., Sanchez-Crispin J.A., Chippaux M. 1986; Tetrathionate reductase of Salmonella typhimurium: a molybdenum-containing enzyme. Biochemical and Biophysical Research Communications 136:577–581
    [Google Scholar]
  13. Johnson J.L. 1980; The molybdenum cofactor common to nitrate reductase, xanthine dehydrogenase and sulphite oxidase. In Molybdenum and Molybdenum-containing Enzymes pp 345–383 Coughlan M. P. Edited by Oxford: Pergamon Press;
    [Google Scholar]
  14. Johnson J.L., Rajagopalan K.V. 1982; Structure and metabolic relationship between the molybdenum cofactor and urothione. Proceedings of the National Academy of Sciences of the United States of America 79:6856–6860
    [Google Scholar]
  15. Krenitsky T.A., Neil S.M., Elion G.B., Hitchings G.H. 1972; A comparison of the specificities of xanthine oxidase and aldehyde oxidase. Archives of Biochemistry and Biophysics 150:585–599
    [Google Scholar]
  16. Krenitsky T.A., Tuttle J.V., Cattau E.L., Wang P. 1974; A comparison of the distribution and electron acceptor specificities of xanthine oxidase and aldehyde oxidase. Comparative Biochemistry and Physiology 49B:687–703
    [Google Scholar]
  17. Lewis N.J., Hurt P., Sealy-Lewis H.M., Scazzocchio C. 1978; The genetic control of the molybdoflavoproteins in Aspergillus nidulans. IV. A comparison between purine hydroxylase I and II. European Journal of Biochemistry 91:311–316
    [Google Scholar]
  18. Massey V. 1973; Iron-sulphur flavoprotein hydroxylases. In Iron-Sulphur Proteins 1 pp 301–360 Lovenberg W. Edited by New York: Academic Press;
    [Google Scholar]
  19. Mehra R.K., Coughlan M.P. 1984; Purification and properties of purine hydroxylase II from Aspergillus nidulans . Archives of Biochemistry and Biophysics 229:585–595
    [Google Scholar]
  20. Nishino T., Nishino T., Tsushima K. 1982; On the nature of the cyanolysable sulphur in xanthine oxidase. In Flavins and Flavoproteins pp 792–795 Massey V., Williams C. H. Edited by Amsterdam: Elsevier;
    [Google Scholar]
  21. Rajagopalan K.V., Handler P. 1964; The absorption spectra of iron flavoproteins. Journal of Biological Chemistry 239:1509–1514
    [Google Scholar]
  22. Scazzocchio C. 1980; The genetics of the molybdenum-containing enzymes. In Molybdenum and Molybdenum-Containing Enzymes pp 487–515 Coughlan M. P. Edited by Oxford: Pergamon Press;
    [Google Scholar]
  23. Scazzocchio C., Sealy-Lewis H.M. 1978; A mutation in the xanthine dehydrogenase (purine hydroxylase I) of Aspergillus nidulans resulting in altered specificity. Implications for the geometry of the active site. European Journal of Biochemistry 91:99–109
    [Google Scholar]
  24. Scazzocchio C., Holl F.B., Foguelman A.I. 1973; The genetic control of molybdoflavoproteins in Aspergillus nidulans. Allopurinol-resistant mutants constitutive for xanthine dehydrogenase. European Journal of Biochemistry 36:428–445
    [Google Scholar]
  25. Turner N., Barata B., Bray R.C., Deistung J., Legall J., Moura J.J.G. 1987; The molybdenum iron-sulphur protein from Desulfovibrio gigas as a form of aldehyde oxidase. Biochemical Journal 243:755–761
    [Google Scholar]
  26. Waud W.R., Rajagopalan K.V. 1976a; Purification and properties of the NAD+-dependent (type D) and (Independent (type O) forms of rat liver xanthine dehydrogenase. Archives of Biochemistry and Biophysics 172:365–379
    [Google Scholar]
  27. Waud W.R., Rajagopalan K.V. 1976b; The mechanism of conversion of rat liver xanthine dehydrogenase from an NAD+-dependent form (type D) to an Oz-dependent form (type O). Archives of Biochemistry and Biophysics 172:354–364
    [Google Scholar]
  28. Waud W.R., Brady F.O., Wiley R.D., Rajagopalan K.V. 1975; A new purification procedure for bovine milk xanthine oxidase: effect of proteolysis on the subunit structure. Archives of Biochemistry and Biophysics 169:695–701
    [Google Scholar]
  29. Wurzinger K.H., Hartenstein R. 1974; Phylogeny and correlations of aldehyde oxidase, xanthine oxidase, xanthine dehydrogenase and peroxidase in animal tissues. Comparative Biochemistry and Physiology 49B:171–185
    [Google Scholar]
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