Chemical keys to molybdenum enzymes[hair space]*

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Edward I. Stiefel


Abstract

Nitrogenase, in which molybdenum is part of a unique multinuclear iron–molybdenum–sulfide cluster, has garnered much deserved attention. However, about 30 other distinct enzymes use molybdenum (and several more use tungsten) in a mononuclear site involving special pterin–ene-dithiolate [pterin = 2-amino-4(1H)-pteridinone, ene-dithiolate = dithiolene] ligation. These molybdenum enzymes have environmental, agronomic, and health relevance. Their ‘molybdenum cofactor’, Moco, is now viewed as a generic term for a family of prosthetic groups, although there are unresolved issues involving nomenclature. Oxygen-atom transfer and proton–electron transfer are convenient ways to stoichiometrically formulate the two-electron substrate and active-site regeneration reactions. Such processes are common in molybdenum chemistry and may have mechanistic relevance. Dithiolene ligands of the type present in Moco are redox active in free or complexed forms. Molybdenum–sulfur systems show facile internal electron–transfer chemistry and partial redox states that have potential structural and mechanistic implications for molybdenum enzymes. Chemical differences between molybdenum and tungsten may influence the respective presence or absence of these elements in enzymes from organisms that occupy diverse habitats.


References

  1. E. I. Stiefel, in Kirk-Othmer Encyclopedia of Chemical Technology, John Wiley and Sons, New York, 1995, vol. 16, p. 940 Search PubMed.
  2. H. Bortels, Zentralbl. Bakteriol. Parisitenkd. Infektionskrankh., 1936, 95, 193 Search PubMed.
  3. R. R. Eady and B. E. Smith, in A Treatise on Nitrogen Fixation, eds. R. W. F. Hardy, F. Bottomley and R. C. Burns, John Wiley and Sons, New York, 1979, vol. I, p. 399 Search PubMed.
  4. J. Kim, D. Woo and D. C. Rees, Biochemistry, 1993, 7104 CrossRef CAS.
  5. J. B. Howard and D. C. Rees, Chem. Rev., 1996, 96, 2965 CrossRef CAS.
  6. R. R. Eady, Sci. Prog. (Oxford), 1995, 78, 1 Search PubMed.
  7. B. K. Burgess and D. J. Lowe, Chem. Rev., 1996, 96, 2983 CrossRef CAS.
  8. R. R. Eady, Chem. Rev., 1996, 96, 3013 CrossRef CAS.
  9. E. C. De Renzo, E. Kaleita, P. G. Heytler, J. J. Oleson, B. L. Hutchings and J. H. Williams, Arch. Biochem. Biophys., 1953, 45, 247 CAS.
  10. E. I. Stiefel, ACS Symp. Ser., 1993, 535, 1 CAS.
  11. R. Hille, JBIC, 1996, 1, 397 CrossRef CAS.
  12. R. Hille, Chem. Rev., 1996, 96, 2757 CrossRef CAS.
  13. J. H. Enemark and C. G. Young, in Advances in Inorganic Chemistry, Academic Press, New York, 1993, vol. 40, p. 1 Search PubMed.
  14. M. K. Johnson, D. C. Rees and M. W. W. Adams, Chem. Rev., 1996, 96, 2817 CrossRef CAS.
  15. A. Kletzin and M. W. W. Adams, FEMS Microbiol. Rev., 1996, 18, 5 CrossRef CAS.
  16. J. C. Wooton, R. E. Nicolson, J. M. Cock, D. E. Walters, J. F. Burke, W. A. Doyle and R. C. Bray, Biochim. Biophys. Acta, 1991, 1057, 157 CAS.
  17. K. V. Rajagopalan and J. L. Johnson, J. Biol. Chem., 1992, 267, 10 199 CAS.
  18. R. S. Pilato and E. I. Stiefel, in Bioinorganic Catalysis, ed. J. Reedijk, Marcel Dekker, New York, 1993, p. 131 Search PubMed.
  19. C. G. Young and A. G. Wedd, in Encyclopedia of Inorganic Chemistry, ed. R. B. King, John Wiley and Sons, New York, 1994, p. 2330 Search PubMed; C. G. Young and A. G. Wedd, Chem. Commun., 1997, 1251 Search PubMed.
  20. D. Collison, C. D. Garner and J. A. Joule, Chem. Soc. Rev., 1996, 25, 25 RSC.
  21. D. C. Rees, Y. Hu, C. Kisker and H. Schindelin, J. Chem. Soc., Dalton Trans., 1997, 3909 RSC.
  22. J. Mason, Toxicology, 1986, 42, 99 CrossRef CAS.
  23. K. M. Weber and R. C. Boston, Aust. J. Agric. Res., 1975, 34, 295 Search PubMed.
  24. S. H. Mudd, F. Irreverre and L. Laster, Science, 1967, 156, 1599 CAS.
  25. J. L. Johnson and K. V. Rajagopalan, J. Clin. Invest., 1976, 58, 551 Search PubMed.
  26. S. Tomita, M. Tsujita and Y. Ichikawa, FEBS Lett., 1993, 336, 272 CrossRef CAS.
  27. B. N. Ames, R. Cathcart, E. Schwiers and P. Hochstein, Proc. Natl. Acad. Sci. USA, 1981, 78, 6858 CAS.
  28. B. F. Becker, Free Radical Biol. Med., 1993, 14, 615 CrossRef CAS.
  29. D. B. Peden, R. Hohman, M. E. Brown, R. T. Mason, C. Berkebile, H. M. Fales and M. A. Kaliner, Proc. Natl. Acad. Sci. USA, 1990, 87, 7638 CAS.
  30. N. S. Mandel and G. S. Mandel, J. Am. Chem. Soc., 1976, 98, 2319 CrossRef CAS.
  31. M. J. Romão, M. Archer, I. Moura, J. J. G. Moura, J. LeGall, R. Engh, M. Schneider, P. Hof and R. Huber, Science, 1995, 270, 1170 CAS.
  32. R. Huber, P. Hof, R. O. Duarte, J. J. Moura, I. Moura, M.-Y. Liu, J. LeGall, R. Hille, M. Archer and M. J. Romão, Proc. Natl. Acad. Sci. USA, 1996, 93, 8846 CrossRef CAS.
  33. H. Schindelin, C. Kisker, J. Hilton, K. V. Rajagopalan and D. C. Rees, Science, 1996, 272, 1615 CrossRef CAS.
  34. F. Schneider, J. Loewe, R. Huber, H. Schindelin, C. Kisker and J. Knaeblein, J. Mol. Biol., 1996, 263, 53 CrossRef CAS.
  35. A. S. McAlpine and S. Bailey, Int. Union Crystallogr. Abstr., Sect. C, 1996 Search PubMed; S. Bailey, A. S. McAlpine and A. G. McEwen, Molybdenum Enzymes Meeting, University of Sussex, UK, April 12–15, 1997, Abstract L15.
  36. J. C. Boyington, V. N. Gladyshev, S. V. Khangulov, T. C. Stadtman and P. D. Sun, Science, 1997, 275, 1305 CrossRef CAS.
  37. C. Kisker, H. Schindelin, D. C. Rees, A. Pacheco and J. Enemark, Molybdenum Enzymes Meeting, University of Sussex, UK, April 12–15, 1997, Abstract P28; G. N. George, C. A. Kipke, R. C. Prince, R. A. Sunde, J. H. Enemark and S. P. Cramer, Biochemistry, 1989, 28, 5075 Search PubMed.
  38. K. V. Rajagopalan, ACS Symp. Ser., 1993, 535, 38 CAS.
  39. S. Gardlik and K. V. Rajagopalan, J. Biol. Chem., 1990, 265, 13 047 CAS.
  40. R. Soyka, W. Pfleiderer and R. Prewo, Helv. Chim. Acta, 1990, 73, 808 CrossRef CAS.
  41. J. L. Johnson, K. V. Rajagopalan, S. Mukund and M. W. W. Adams, J. Biol. Chem., 1993, 268, 4848 CAS.
  42. M. K. Chan, S. Mukund, A. Kletzin, M. W. W. Adams and D. C. Rees, Science, 1995, 267, 1463 CAS.
  43. E. I. Stiefel, Proc. Natl. Acad. Sci. USA, 1973, 70, 988 CAS.
  44. R. H. Holm, Coord. Chem. Rev., 1990, 100, 183 CrossRef CAS.
  45. E. I. Stiefel, Prog. Inorg. Chem., 1977, 22, 1.
  46. E. I. Stiefel, in Comprehensive Coordination Chemistry, eds. G. Wilkinson, R. D. Gillard and J. A. McCleverty, Pergamon, New York, 1987, vol. 3, p. 1375 Search PubMed.
  47. B. A. Moyer and T. J. Meyer, Inorg. Chem., 1981, 20, 436 CrossRef CAS.
  48. R. Hille and H. Sprecher, J. Biol. Chem., 1987, 262, 10 914 CAS.
  49. A. K. Rappé and W. A. Goddard III, Nature (London), 1980, 285, 311 CrossRef CAS.
  50. J. A. McCleverty, Prog. Inorg. Chem., 1968, 10, 49 CAS.
  51. R. Eisenberg, Prog. Inorg. Chem., 1970, 12, 295 CAS.
  52. R. P. Burns and C. A. McAuliffe, Adv. Inorg. Chem. Radiochem., 1979, 22, 303 Search PubMed.
  53. H. Oku, N. Ueyama and A. Nakamura, Chem. Lett., 1996, 1131 CAS.
  54. H. Oku, N. Ueyama and A. Nakamura, Chem. Lett., 1996, 31 CAS.
  55. N. Ueyama, H. Oku, M. Kondo, T.-A. Okamura, N. Yoshinaga and A. Nakamura, Inorg. Chem., 1996, 35, 643 CrossRef CAS.
  56. S. K. Das, P. K. Chaudhury, D. Biswas and S. Sarkar, J. Am. Chem. Soc., 1994, 116, 9061 CrossRef CAS.
  57. S. Sarkar and S. K. Das, Proc. Indian Acad. Sci., Chem. Sci., 1992, 104, 437 Search PubMed.
  58. J. Yadav, S. K. Das and S. Sarkar, J. Am. Chem. Soc., 1997, 119, 4315 CrossRef CAS.
  59. W. H. Pan, T. R. Halbert, L. L. Hutchings and E. I. Stiefel, J. Chem. Soc., Chem. Commun., 1985, 927 RSC.
  60. Y. Gea, M. A. Greaney, C. L. Coyle and E. I. Stiefel, J. Chem. Soc., Chem. Commun., 1992, 160 RSC.
  61. H. H. Murray, L. Wei, S. E. Sherman, M. A. Greaney, K. A. Eriksen, B. Cartensen, T. R. Halbert and E. I. Stiefel, Inorg. Chem., 1995, 34, 841 CrossRef CAS.
  62. L. Wei, T. R. Halbert, H. H. Murray, III and E. I. Stiefel, J. Am. Chem. Soc., 1990, 112, 6431 CrossRef CAS.
  63. T. R. Halbert, L. L. Hutchings, R. Rhodes and E. I. Stiefel, J. Am. Chem. Soc., 1986, 108, 6437 CrossRef CAS.
  64. J. Bernholc and E. I. Stiefel, Inorg. Chem., 1985, 24, 1323 CrossRef CAS.
  65. A. B. P. Lever, Inorganic Electronic Spectroscopy, Elsevier, New York, 1984 Search PubMed.
  66. L. G. Ljungdahl, Trends Biochem. Sci., 1976, 1, 63 CAS.
  67. L. G. Ljungdahl and J. R. Andreesen, Methods Enzymol., 1978, 53, 360 CrossRef CAS.
  68. E. I. Stiefel, D. Coucouvanis and W. E. Newton(Editors), ACS Symp. Ser., 1993, 535 Search PubMed.
  69. C. D. Garner, E. M. Armstrong, M. J. Ashcroft, M. S. Austerberry, J. H. Birks, D. Collison, A. J. Goodwin, L. Larsen, D. J. Rowe and J. R. Russell, ACS Symp. Ser., 1993, 535, 98 CAS.
  70. R. S. Pilato, K. Eriksen, M. A. Greaney, Y. Gea, E. C. Taylor, S. Goswami, L. Kilpatrick, T. G. Spiro, A. L. Rheingold and E. I. Stiefel, ACS Symp. Ser., 1993, 535, 83 CAS.
  71. R. S. Pilato, K. A. Eriksen, M. A. Greaney, E. I. Stiefel, S. Goswami, L. Kilpatrick, T. G. Spiro, E. C. Taylor and A. L. Rheingold, J. Am. Chem. Soc., 1991, 113, 9372 CrossRef CAS.
  72. A. F. Arendsen, M. de Vocht, Y. B. M. Bulsink and W. R. Hagen, J. Biol. Inorg. Chem., 1996, 1, 292 CrossRef CAS.
  73. E. I. Stiefel, Z. Dori and H. B. Gray, J. Am. Chem. Soc., 1967, 89, 3353 CrossRef CAS.
  74. E. I. Stiefel, K. F. Miller, A. E. Bruce, J. L. Corbin, J. M. Berg and K. O. Hodgson, J. Am. Chem. Soc., 1980, 102, 3624 CrossRef CAS.
  75. J. M. Berg, D. J. Spira, K. O. Hodgson, A. E. Bruce, K. F. Miller, J. L. Corbin and E. I. Stiefel, Inorg. Chem., 1984, 23, 3412 CrossRef CAS.
  76. A. A. Eagle, L. J. Laughlin, C. G. Young and E. R. T. Tiekink, J. Am. Chem. Soc., 1992, 114, 9195 CrossRef CAS.
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