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Structure and function of the xanthine-oxidase family of molybdenum enzymes

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Metal Sites in Proteins and Models Redox Centres

Part of the book series: Structure & Bonding ((4143,volume 90))

Abstract

This work gives an account of the recent achievements which have contributed towards the understanding of the structure and function of the xanthine oxidase family of enzymes-the molybdenum hydroxylases. It is based essentially on the crystallographic data of the aldehyde oxido-reductase from Desulfovibrio (D.) gigas, a member of that family, whose structure is described in detail. Comparisons are made, whenever appropriate, with spectroscopic, kinetic and model compound studies. Mechanistic implications of the crystal structure of the D. gigas enzyme are considered and extended to the xanthine oxidase family.

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Abbreviations

AOR:

aldehyde ferredoxin oxido-reductase from Pyrococcus furiosus

DMSOR:

dimethylsulfoxide reductase

Mop:

aldehyde oxido-reductase from Desulfovibrio gigas

Mod:

aldehyde oxido-reductase from Desulfovibrio desulfuricans ATCC27774

MPT:

mononucleotide form of molybdopterin

MCD:

molybdopterin cytosine dinucleotide

MGD:

molybdopterin guanine dinucleotide

MAD:

molybdopterin adenine dinucleotide

MHD:

molybdopterin hypoxanthine dinucleotide

XO:

xanthine oxidase

XDH:

xanthine dehydrogenase

References

  1. Rees DC, Kim J, Georgiadis MM, Komiya H, Chirino AJ, Woo D, Schlessman J, Chan MK, Joshua-Tor L, Santillan G, Chakrabarti, Hsu BT (1993) ACS Symposia 535:170

    CAS  Google Scholar 

  2. Holm, RH (1987) Chem Rev 87:1401

    CAS  Google Scholar 

  3. Hille R (1996) Chem Rev (in press)

    Google Scholar 

  4. Murray, KN, Watson JG, Chaykin S (1966) J Biol Chem 241:4798

    PubMed  CAS  Google Scholar 

  5. Wooton JC, Nicolson RE, Cock JM, Walters DE, Burke JF, Doyle WA, Bray RC (1991) Biochim Biophys Acta 1057:1575

    Google Scholar 

  6. Romão MJ, Archer M, Moura I, Moura JJG, LeGall J, Engh R, Schneider M, Hof P, Huber R (1995) Science 167:1167

    Google Scholar 

  7. Hille R (1994) Biochim Biophys Acta 1994:143

    Google Scholar 

  8. Cramer SP, Hille R (1985) J Am Chem Soc 107:8164

    CAS  Google Scholar 

  9. Hille R, George GN, Eidsness MK, Cramer SP (1989) Inorg Chem 28:4018

    CAS  Google Scholar 

  10. Bray RC (1988) Quaterly Rev Biophysics 21:299

    CAS  Google Scholar 

  11. Turner N, Barata BAS, Bray RC, Deistung J, LeGall J, Moura JJG (1987) Biochem J 243:755

    PubMed  CAS  Google Scholar 

  12. Johnson JL, Hairline BE, Rajagopalan KV (1980) J Biol Chem 255:1783

    PubMed  CAS  Google Scholar 

  13. Johnson JL, Rajagopalan KV (1982) Proc Natl Acad Sci USA 79:6856

    PubMed  CAS  Google Scholar 

  14. Johnson JL, Hairline BE, Rajagopalan KV, Arison BH (1984) J Biol Chem 259:5414

    PubMed  CAS  Google Scholar 

  15. Cramer SP, Johnson JL, Ribeiro AA, Millington DS, Rajagopalan KV (1987) J Biol Chem 262:16357; b) Johnson JL, Wuebbens MM, Rajagopalan KV (1989) J Biol Chem 264: 13440; c) Rajagopalan KV, Johnson JL (1992) J Biol Chem 267:10199

    Google Scholar 

  16. Chan MK, Mukund S, Kletzin A, Adams MWW, Rees DC (1995) Science 267:1463

    PubMed  CAS  Google Scholar 

  17. Johnson JL, Bastian NR, Rajagopalan KV (1990) Proc Natl Acad Aci USA 87:3190

    CAS  Google Scholar 

  18. Börner G, Karrasch K, Thauer RK (1991) FEBS Lett 290:31

    PubMed  Google Scholar 

  19. Thoenes U, Flores OL, Neves A, Devreese B, Beeumen JJV, Huber R, Romão MJ, LeGall J, Moura JJG, Rodrigues-Pousada C (1994) Eur J Biochem 220:901

    PubMed  CAS  Google Scholar 

  20. Meyer O (1982) J Biol Chem 257:1333

    PubMed  CAS  Google Scholar 

  21. Krüger B, Meyer O (1986) Fur J Biochem 157:121

    Google Scholar 

  22. Schiibel U, Kraut M, Mbrsdorf G, Meyer O (1995) J Bacteriol 177:2197

    Google Scholar 

  23. Tchisuaka B, Kappl R, Hilttermann J, Lingens F(1993) Biochem 32:12928

    Google Scholar 

  24. Peschke B, Lingens F (1990) Biol Chem Hoppe-Seyler 372:1081

    Google Scholar 

  25. Schach S, Tchisuaka B, Fetzner S, Lingens F (1995) Eur J Biochem 232:536

    PubMed  CAS  Google Scholar 

  26. Lehmann R, Tchisuaka B, Fetzner S, Röger P, Lingens F (1994) J Biol Chem 269:11254

    PubMed  CAS  Google Scholar 

  27. Bauer G, Lingens F (1992) Biol Chem Hoppe-Seyler 373:699

    PubMed  CAS  Google Scholar 

  28. Fetzner S, Lingens F (1993) Biol Chem Hoppe-Seyler 374:363

    PubMed  CAS  Google Scholar 

  29. Sauter M, Tchisuaka B, Fetzner S, Lingens F (1993) Biol Chem Hoppe-Seyler 374:1037

    PubMed  CAS  Google Scholar 

  30. Dilworth GL (1982) Arch Biochem Biophys 219:30

    PubMed  CAS  Google Scholar 

  31. Nagel M, Andreesen JR (1990) Arch Microbiol 154:605

    CAS  Google Scholar 

  32. Freudenberg W, König K, Andreesen JR (1988) FEMS Microbiol Lett 52:13

    CAS  Google Scholar 

  33. Grether-Beck S, Iglio GL, Pust S, Schilz E, Decker K, Brandsch R (1994) Mol Microbiol 13:929

    PubMed  CAS  Google Scholar 

  34. Holm RH (1990) Coord Chem Rev 100:183

    CAS  Google Scholar 

  35. Enemark JH, Young CG (1993) Adv Inorg Chem 40:1

    Google Scholar 

  36. Bhattacharyya A, Tollin G, Davis M, Edmonson DE (1983) Biochem 22:5270

    CAS  Google Scholar 

  37. Walker MC, Hazzard JT, Tollin G, Edmonson DE (1991) Biochem 30:5912

    CAS  Google Scholar 

  38. Anderson RF, Hille R, Massey V (1986) J Biol Chem 261:15870

    PubMed  CAS  Google Scholar 

  39. Hille R, Anderson RF (1991) J Biol Chem 266:5608

    PubMed  CAS  Google Scholar 

  40. Porras AG, Palmer G (1982) J Biol Chem 257:11617

    PubMed  CAS  Google Scholar 

  41. Barber, MJ, Siegel LM (1982) Biochem 21:1638

    CAS  Google Scholar 

  42. Hille R, Massey V (1986) J Biol Chem 261:1241

    PubMed  CAS  Google Scholar 

  43. George GN, Bray RC (1983) Biochem 22:1013

    CAS  Google Scholar 

  44. Hille R, Stewart RC, Fee JA, Massey (1983) J Biol Chem 258:4849

    PubMed  CAS  Google Scholar 

  45. Barber, MJ, Siegel LM (1983) Biochem 22:618

    CAS  Google Scholar 

  46. Barber MJ, Coughlan MP, Rajagopalan KV, Siegel LM (1982) Biochemistry 21:3561

    PubMed  CAS  Google Scholar 

  47. Lowe DJ, Barber MJ, Pawlik RT, Bray RC (1976) Biochem J 155:81

    PubMed  CAS  Google Scholar 

  48. Hawkes TR, George GN, Bray RC (1984) Biochem J 218:961

    PubMed  CAS  Google Scholar 

  49. Gutteridge S, Tanner SJ, Bray RC (1978) Biochem J 175:869

    PubMed  CAS  Google Scholar 

  50. Gutteridge S, Tanner SJ, Bray RC (1978) Biochem J 175:887

    PubMed  CAS  Google Scholar 

  51. Gibson JF, Bray RC (1968) Biochim Biophys Acta 153:721

    PubMed  CAS  Google Scholar 

  52. Bray RC, Turner NA, LeGall J, Barata BAS, Moura JJG (1991) Biochem J 280:817

    PubMed  CAS  Google Scholar 

  53. Lowe DJ, Lynden-Bell RM, Bray RC (1972) Biochem J 130:239

    PubMed  CAS  Google Scholar 

  54. Morpeth FF, George GN, Bray RC (1984) Biochem J 220:235

    PubMed  CAS  Google Scholar 

  55. Barata BAS, Liang J, Moura I, LeGall J, Moura JJG, Hanh Huynh B (1992) Eur J Biochem 204,773

    PubMed  CAS  Google Scholar 

  56. Huber R, Duarte R, Moura I, Moura JJG, LeGall J, Liu M, Hille R, Romao MJ (1996) Proc Natl Acad Sci USA, 93:8846

    PubMed  CAS  Google Scholar 

  57. Turner NA, Bray RC, Diakun GP (1989) Biochem J 260:563

    PubMed  CAS  Google Scholar 

  58. Cramer SP, Moura JJG, Xavier AV, LeGall J (1984) J Inorg Biochem 20:275

    PubMed  CAS  Google Scholar 

  59. Schindelin H, Kisker C, Hilton J, Rajagopalan KV, Rees DC (1996) Science 272:1615

    PubMed  CAS  Google Scholar 

  60. Stiefel EI (1993) ACS Symposia 535:1

    CAS  Google Scholar 

  61. Hille R (1993) ACS Symposia 535:22

    CAS  Google Scholar 

  62. Romão MJ, Barata BAS, Lobeck K, Moura I, Carrondo MA, LeGall J, Lottspeich F, Huber R, Moura JJG (1993) Eur J Biochem 215:729

    PubMed  Google Scholar 

  63. Moura JJG, Xavier AV, Bruschi M, LeGall J, Hall DO, Cammack R (1976) Biochem Biophys Res Commun 72:782

    PubMed  CAS  Google Scholar 

  64. Caldeira J, Moura I, Romão MJ, Huber R, LeGall J, Moura JJG (1995) J Inorg Biochem 59: 739

    Google Scholar 

  65. Schneider F, Löwe J, Huber R, Schindelin H, Kisker C, Knäblein J (1996) J Mol Biol (in press)

    Google Scholar 

  66. Fukuyama K, Hase T, Matsumoto S, Tsukihara T, Katsube Y, Tanaka N, Kakudo M, Wada K, Matsubara H (1980) Nature 286:522; (b) Tsukihara T, Fukuyama K, Nakamura M, Katsube Y, Tanaka N, Kakudo M, Wada K, Hase T, Matsubara H (1981) J Biochem 90:1763 67. Barata BAS, LeGall J, Moura JJG (1993) Biochemistry 32:11559

    CAS  Google Scholar 

  67. Fischer B, Schmalle H, Dubler E, Schäfer A, Viscontini M (1995) Inorg Chem 34:5726

    CAS  Google Scholar 

  68. Moura JJG, Xavier AV, Cammack R, Hall DO, Bruschi M, LeGall J (1978) Biochem J 173:419

    PubMed  CAS  Google Scholar 

  69. Olson JS, Ballou DP, Palmer G, Massey V (1974) J Biol Chem 249:4363

    PubMed  CAS  Google Scholar 

  70. Gardlik S, Rajagopalan KV (1990) J Biol Chem 265:13047

    PubMed  CAS  Google Scholar 

  71. Gardlik S, Rajagopalan KV (1991) J Biol Chem 266:4889

    PubMed  CAS  Google Scholar 

  72. Burgmayer SJN, Baruch A, Kerr K, Yoon K (1989) J Am Chem Soc 111:4982

    CAS  Google Scholar 

  73. Stiefel EI, Miller KF, Bruce AE, Corbin JL, Berg JM, Hodgson KO (1980) J Am Chem Soc 102:3624

    CAS  Google Scholar 

  74. Doyle W, Chovnick A, Whittle JRS, Bray RC (1996) Biochem Soc Trans 24:14S

    PubMed  CAS  Google Scholar 

  75. Bray RC, Bennett B, Burke JF, Chovnick A, Doyle WA, Howes BD, Lowe DJ, Richards RL, Turner NA, Ventom A, Whittle JRS (1996) Biochem Soc Trans 24:99

    PubMed  CAS  Google Scholar 

  76. Hilton JC, Rajagopalan KV (1996) Archives Biochem Biophys 325:139

    CAS  Google Scholar 

  77. Lowe DJ, Bray RC (1978) Biochem J 169:471

    PubMed  CAS  Google Scholar 

  78. Barber MJ, Salerno JC, Siegel LM (1982) Biochemistry 21:1648

    PubMed  CAS  Google Scholar 

  79. Tsukihara T, Fukuyama K, Mizushima M, Harioka T, Kusunoki M, Katsube Y, Hase T, Matsubara H (1990) J Mol Biol 216:399

    PubMed  CAS  Google Scholar 

  80. Rypniewski R, Breiter DR, Benning MM, Wesenberg G, Oh BH, Markley JL, Rayment I, Holden HM (1991) Biochemistry 30:4126

    PubMed  CAS  Google Scholar 

  81. Burgmayer SJN, Arkin MR, Bostick L, Dempster S, Everett KM, Layton HL, Paul KE, Rogge C, Rheingold AL (1995) J Am Chem Soc 117:5812

    CAS  Google Scholar 

  82. Hughes RK, Doyle WA, Chovnick A, Whittle JRS, Burke JF, Bray RC (1992) Biochem J 285:507

    PubMed  CAS  Google Scholar 

  83. Sato A, Nishino T, Noda K, Amaya Y, Nishino T (1995) J Biol Chem 270:2818

    PubMed  CAS  Google Scholar 

  84. Doyle WA, Burke JF, Chovnick A, Dutton FL, Russell C, Whittle JRS, Bray RC (1996) Biochem Soc Trans 24:315

    Google Scholar 

  85. Nishino T, Nishino T (1989) J Biol Chem 264:5468

    PubMed  CAS  Google Scholar 

  86. Turner NA, Doyle WA, Ventom AM, Bray RC (1995) Eur J Biochem 232:646

    PubMed  CAS  Google Scholar 

  87. Nishino T, Tsushima K, Hille R, Massey V (1982) J Biol Chem 257:7348; b) Nishino T, Amaya Y, Nishino T (1990) 10th International Symposium on Flavins and Flavoproteins, Como, Italy

    PubMed  CAS  Google Scholar 

  88. Burgmayer SJN, Everett K, Bostick L (1993) ACS Symposia 535:114

    CAS  Google Scholar 

  89. Greenwood RJ, Wilson GL, Pilbrow J R, Wedd A G (1993) J Am Chem Soc 115:5385

    CAS  Google Scholar 

  90. Tanner SJ, Bray RC (1978) Biochem Soc Trans 6:1331

    PubMed  CAS  Google Scholar 

  91. Morpeth FF, Bray RC (1984) Biochemistry 23:1332

    PubMed  CAS  Google Scholar 

  92. Scazzocchio C, Sealy-Lewis HM (1978) Eur J Biochem 91:99

    PubMed  CAS  Google Scholar 

  93. Glatigny A, Scazzocchio C (1995) J. Biol Chem 270:3534

    PubMed  CAS  Google Scholar 

  94. Pick FM, McGartoll MA, Bray RC (1971) Eur J Biochem 18:65

    PubMed  CAS  Google Scholar 

  95. Hille R, Kim JH, Hemann C (1993) Biochemistry 32:3973

    PubMed  CAS  Google Scholar 

  96. Hille R, Stewart RC (1984) J Biol Chem 259:1570

    PubMed  CAS  Google Scholar 

  97. Howes BD, Bray RC, Richards RL, Turner NA, Bennett B, Lowe DJ (1996) Biochemistry 35:1432; b) Howes BD, Bennett B, Bray RC, Richards RL, Lowe DJ (1994) J Am Chem Soc 116:11624

    PubMed  CAS  Google Scholar 

  98. Bray RC, George GN (1985) Biochem Soc Trans 13:560

    PubMed  CAS  Google Scholar 

  99. Rappé AK, Goddard WA III (1982) J Am Chem Soc 104:3287

    Google Scholar 

  100. Collison D, Garner CD, Joule JA (1996) Chem Soc Rev: 25

    Google Scholar 

  101. Kim JH, Ryan MG, Knaut H, Hille R (1996) J Biol Chem 271:6771

    PubMed  CAS  Google Scholar 

  102. Terao M, Cazzaniga G, Ghezz P, Bianchi M, Falciani F, Perani P, Garattini E (1992) Biochem J 283:863

    PubMed  CAS  Google Scholar 

  103. Amaya Y, Yamazaki K, Sato M, Noda K, Nishino T, Nishino T (1990) J Biol Chem 265:14170

    PubMed  CAS  Google Scholar 

  104. Houde M, Tiveron MC, Bregegere F (1988) EMBL data library

    Google Scholar 

  105. Lehmann R, Tchisuaka B, Fetzner S, Lingens F (1995) J Biol Chem 270:14420

    PubMed  CAS  Google Scholar 

  106. Lee CS, Curtis D, McCarron M, Love C, Gray H, Bander W, Chovnick A (1987) Genetics 116:55

    PubMed  CAS  Google Scholar 

  107. Yasokochi Y, Kanda T, Tamura T, unpublished

    Google Scholar 

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Authors and Affiliations

  1. Instituto de Tecnologia Química e Biológica, Apt. 127, 2780 Oeiras and Instituto Superior Técnico, Dep. Química, 1096 Lisboa Codex, Portugal

    Maria João Romão

  2. Max-Planck-Institut für Biochemie, am Klopferspitz 18a, D-82152, Martinsried, Germany

    Robert Huber

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  1. Maria João Romão
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  2. Robert Huber
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Correspondence to Maria João Romão .

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H. A. O. Hill P. J. Sadler A. J. Thomson

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Romão, M.J., Huber, R. (1998). Structure and function of the xanthine-oxidase family of molybdenum enzymes. In: Hill, H.A.O., Sadler, P.J., Thomson, A.J. (eds) Metal Sites in Proteins and Models Redox Centres. Structure & Bonding, vol 90. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3-540-62888-6_3

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  • DOI: https://doi.org/10.1007/3-540-62888-6_3

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