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General references on structure and function of molybdopterin­containing proteins

  1. Adams, M.W.W. and Mortenson, L.E. (1985) Mo reductases: Nitrate reductase and formate dehydrogenase. In Spiro, T.G., Ed. Molybdenum Enzymes. Wiley, New York, pp. 519-593.
  2. Barrett, E.L. and Kwan, H.S. (1985) Bacterial reduction of trimethylamine oxide. Annu. Rev. Microbiol. 39, 131-149.
  3. Begley, T.P., Kinsland, C., Taylor, S., Tandon, M., Nicewonger, R., Wu, M., Chiu, H.­J., Kelleher, N., Campobasso, N. and Zhang, Y. (1998) Cofactor biosynthesis: A mechanistic perspective. Topics in Current Chemistry 195, 93-142.
  4. Bray, R.C. and Swann, J.C. (1972) Molybdenum­containing enzymes. Structure and Bonding 11, 107-144.
  5. Burgmayer, S.J.N. (1998) Electron transfer in transition metal-pteridine systems. Structure and Bonding 92, 67-119.
  6. Cramer, S.P. and Stiefel, E.I. (1985) Chemistry and biology of the molybdenum cofactor. In Spiro, T.G., Ed. Molybdenum Enzymes. Wiley, New York, pp. 411-441.
  7. Enemark, J.H. and Garner, C.D. (1997) The coordination chemistry and function of the molybdenum centres of the oxomolybdoenzymes. J. Biol. Inorg. Chem. 2, 817-822.
  8. Ferry, J.G. (1990) Formate dehydrogenase. FEMS Microbiol. Rev. 7, 377-382.
  9. Fischer, B., Schmalle, H., Dubler, E. and Viscontini, M. (1993) Molybdenum-pterin complexes: a functional and structural model for the binding site in the enzyme dimethyl sulfoxide reductase. Adv. Exp. Med. Biol. 338, 369-372.
  10. Garner, C.D. and Bristow, S. (1985) Oxomolybdenum chemistry in relation to the molybdoenzymes. In Spiro, T.G., Ed. Molybdenum Enzymes. Wiley, New York, pp. 343-410.
  11. George, G.N. (1997) X­ray absorption spectroscopy of molybdenum enzymes. J. Biol. Inorg. Chem. 2, 790-796.
  12. Hagen, W.R. and Arendsen, A.F. (1998) The bio­inorganic chemistry of tungsten. Structure and Bonding 90, 161-192.
  13. Hille, R. (1996a) Structure and function of mononuclear molybdenum enzymes. J. Biol. Inorg. Chem. 1, 397-404.
  14. Hille, R. (1996b) The mononuclear molybdenum enzymes. Chem. Rev. 96, 2757-2816.
  15. Hille, R. (1997) Mechanistic aspects of the mononuclear molybdenum enzymes. J. Biol. Inorg. Chem. 2, 804-809.
  16. Hille, R. and Massey, V. (1981) Tight binding inhibitors of xanthine oxidase. Pharmacol. Ther. 14, 249-263.
  17. Hille, R. and Massey, V. (1985) Molybdenum­containing hydroxylases: Xanthine oxidase, aldehyde oxidase, and sulfite oxidase. In Spiro, T.G., Ed. Molybdenum Enzymes. Wiley, New York, pp. 443-518.
  18. Johnson, J.L., Rajagopalan, K.V. and Wadman, S.K. (1993) Human molybdenum cofactor deficiency. Adv. Exp. Med. Biol. 338, 373-378.
  19. Johnson, M.K., Rees, D.C. and Adams, M.W.W. (1996) Tungstoenzymes. Chem. Rev. 96, 2817-2839.
  20. Johnson, M.K., Garton, S.D. and Oku, H. (1997) Resonance Raman as a direct probe for the catalytic mechanism of molybdenum oxotransferases. J. Biol. Inorg. Chem. 2, 797-803.
  21. Kisker, C., Schindelin, H. and Rees, D.C. (1997) Molybdenum­cofactor-containing enzymes: structure and mechanism. Annu. Rev. Biochem. 66, 233-267.
  22. Kletzin, A. and Adams, M.W.W. (1996) Tungsten in biological systems. FEMS Microbiol. Rev. 18, 5-63.
  23. McEwan, A.G., Benson, N., Bonnett, T.C., Hanlon, S.P., Ferguson, S.J., Richardson, D.J. and Jackson, J.B. (1991) Bacterial dimethyl sulphoxide reductases and nitrate reductases. Biochem. Soc. Trans. 19, 605-608.
  24. McMaster, J. and Enemark, J.H. (1998) The active sites of molybdenum­ and tungsten­containing enzymes. Curr. Opin. Chem. Biol. 2, 201-207.
  25. Nichol, C.A., Smith, G.K. and Duch, D.S. (1985) Biosynthesis and metabolism of tetrahydrobiopterin and molybdopterin. Annu. Rev. Biochem. 54, 729-764.
  26. Nomenclature Committee of the International Union of Biochemistry (NC-IUB) (1991) Nomenclature of electron­transfer proteins. Recommendations 1989. Eur. J. Biochem. 200, 599-611.
  27. Rajagopalan, K.V. (1988) Molybdopterin - problems and perspectives. BioFactors 1, 273-278.
  28. Rajagopalan, K.V. (1997a) The molybdenum cofactors - perspective from crystal structure. J. Biol. Inorg. Chem. 2, 786-789.
  29. Rajagopalan, K.V. (1997b) Biosynthesis and processing of the molybdenum cofactors. Biochem. Soc. Trans. 25, 757-761.
  30. Rajagopalan, K.V., Johnson, J.L., Wuebbens, M.M., Pitterle, D.M., Hilton, J.C., Zurick, T.R. and Garrett, R.M. (1993) Chemistry and biology of the molybdenum cofactors. Adv. Exp. Med. Biol. 338, 355-362.
  31. Reeve, J.N., Nölling, J., Morgan, R.M. and Smith, D.R. (1997) Methanogenesis: genes, genomes, and who's on first? J. Bacteriol. 179, 5975-5986.
  32. Schindelin, H., Kisker, C. and Rees, D.C. (1997) The molybdenum­cofactor: a crystallographic perspective. J. Biol. Inorg. Chem. 2, 773-781.
  33. Shanmugam, K.T., Stewart, V., Gunsalus, R.P., Boxer, D.H., Cole, J.A., Chippaux, M., DeMoss, J.A., Giordano, G, Lin, E.C. and Rajagopalan, K.V. (1992) Proposed nomenclature for the genes involved in molybdenum metabolism in Escherichia coli and Salmonella typhimurium. Mol. Microbiol. 6, 3452-3454.
  34. Stouthamer, A.H. (1991) Metabolic regulation including anaerobic metabolism in Paracoccus denitrificans. J. Bioenerg. Biomembr. 23, 163-185.
  35. Wootton, J.C., Nicolson, R.E., Cock, J.M., Walters, D.E., Burke, J.F., Doyle, W.A. and Bray, R.C. (1991) Enzymes depending on the pterin molybdenum cofactor: Sequence families, spectroscopic properties of molybdenum and possible cofactor­binding domains. Biochim. Biophys. Acta 1057, 157-185.
  36. Young, C.G. (1997) Models for the molybdenum hydroxylases. J. Biol. Inorg. Chem. 2, 810-816.
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