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Bibliography on structural studies of xanthine oxidase family

  1. Anderson, R.F., Hille, R. and Massey, V. (1986) The radical chemistry of milk xanthine oxidase as studied by radiation chemistry techniques. J. Biol. Chem. 261, 15870-15876.
  2. Anderson, R.F., Hille, R. and Patel, K.B. (1995) Inactivation of xanthine oxidase by oxidative radical attack. Int. J. Radiat. Biol. 68, 535-541.
  3. Barata, B.A.S., Liang, J., Moura, I., LeGall, J., Moura, J.J.G. and Huynh, B.­H. (1992) Mössbauer study of the native, reduced and substrate­reacted Desulfovibrio gigas aldehyde oxido­reductase. Eur. J. Biochem. 204, 773-778.
  4. Barber, M.J. and Siegel, L.M. (1983) Electron paramagnetic resonance and potentiometric studies of arsenite interaction with the molybdenum centers of xanthine oxidase, xanthine dehydrogenase, and aldehyde oxidase: A specific stabilization of the molybdenum(V) oxidation state. Biochemistry 22, 618-624.
  5. Barber, M.J., Bray, R.C., Lowe, D.J. and Coughlan, M.P. (1976) Studies by electron­paramagnetic­resonance spectroscopy and stopped­flow spectrophotometry on the mechanism of action of turkey liver xanthine dehydrogenase. Biochem. J. 153, 297-307.
  6. Barber, M.J., Bray, R.C., Cammack, R. and Coughlan, M.P. (1977) Oxidation-reduction potentials of turkey liver xanthine dehydrogenase and the origins of oxidase and dehydrogenase behaviour in molybdenum­containing hydroxylases. Biochem. J. 163, 279-289.
  7. Barber, M.J., Salerno, J.C. and Siegel, L.M. (1982a) Magnetic interactions in milk xanthine oxidase. Biochemistry 21, 1648-1656.
  8. Barber, M.J., Coughlan, M.P., Rajagopalan, K.V. and Siegel, L.M. (1982b) Properties of the prosthetic groups of rabbit liver aldehyde oxidase: A comparison of molybdenum hydroxylase enzymes. Biochemistry 21, 3561-3568.
  9. Bordas, J., Bray, R.C., Garner, C.D., Gutteridge, S. and Hasnain, S.S. (1979) EXAFS studies of the molybdenum center of xanthine oxidase. J. Inorg. Biochem. 11, 181-186.
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  11. Bray, R.C. and Gutteridge, S. (1982) Numbers and exchangeability with water of oxygen­17 atoms coupled to molybdenum (V) in different reduced forms of xanthine oxidase. Biochemistry 21, 5992-5999.
  12. Bray, R.C. and Meriwether, L.S. (1966) Electron spin resonance of xanthine oxidase substituted with molybdenum­95. Nature 212, 467-469.
  13. Bray, R.C. and Vänngård, T. (1969) "Rapidly appearing" molybdenum electron­paramagnetic­resonance signals from reduced xanthine oxidase. Biochem. J. 114, 725-734.
  14. Bray, R.C., Knowles, P.F., Pick, F.M. and Vänngård, T. (1968) Electron­spin­resonance evidence for interaction of protons with Mo(V) in reduced forms of xanthine oxidase. Biochem. J. 107, 601-602.
  15. Bray, R.C., Barber, M.J. and Lowe, D.J. (1978) Electron­paramagnetic­resonance spectroscopy of complexes of xanthine oxidase with xanthine and uric acid. Biochem. J. 171, 653-658.
  16. Bray, R.C., Gutteridge, S., Stotter, D.A. and Tanner, S.J. (1979) The mechanism of action of xanthine oxidase. The relationship between the rapid and very rapid molybdenum electron­paramagnetic­resonance signals. Biochem. J. 177, 357-360.
  17. Bray, R.C., George, G.N., Gutteridge, S., Norlander, L., Stell, J.G. and Stubley, C. (1982) Studies by electron­paramagnetic­resonance spectroscopy of the molybdenum centre of aldehyde oxidase. Biochem. J. 203, 263-267.
  18. Bray, R.C., Turner, N.A., LeGall, J., Barata, B.A.S. and Moura, J.J.G. (1991) Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas. Biochem. J. 280, 817-820.
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  20. Canne, C., Stephan, I., Finsterbusch, J., Lingens, F., Kappl, R., Fetzner, S. and Huttermann, J. (1997) Comparative EPR and redox studies of three prokaryotic enzymes of the xanthine oxidase family: quinoline 2­oxidoreductase, quinaldine 4­oxidase, and isoquinoline 1­oxidoreductase. Biochemistry 36, 9780-9790.
  21. Conrads, T., Hemann, C. and Hille, R. (1998) Formation of a tyrosyl radical in xanthine oxidase. Biochemistry 37, 7787-7791.
  22. Coughlan, M.P., Betcher­Lange, S.L. and Rajagopalan, K.V. (1979) Isolation of the domain containing the molybdenum, iron-sulfur I, and iron-sulfur II centers of chicken liver xanthine dehydrogenase. J. Biol. Chem. 254, 10694-10699.
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  24. Coughlan, M.P., Mehra, R.K., Barber, M.J. and Siegel, L.M. (1984) Optical and electron paramagnetic resonance spectroscopic studies on purine hydroxylase II from Aspergillus nidulans. Arch. Biochem. Biophys. 229, 596-603.
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  26. Cramer, S.P., Moura, J.J.G., Xavier, A.V. and LeGall, J. (1984) Molybdenum EXAFS of the Desulfovibrio gigas Mo(2Fe-2S) protein - Structural similarity to "desulfo" xanthine dehydrogenase. J. Inorg. Biochem. 20, 275-280.
  27. Dalton, H., Lowe, D.J., Pawlik, T. and Bray, R.C. (1976) Studies by electron­paramagnetic­resonance spectroscopy on the mechanism of action of xanthine dehydrogenase from Veillonella alcalescens. Biochem. J. 153, 287-295.
  28. Duarte, R.O., Reis, A.R., Girio, F., Moura, I., Moura, J.J.G. and Collaco, T.A. (1997) The formate dehydrogenase isolated from the aerobe Methylobacterium sp. RXM is a molybdenum­containing protein. Biochem. Biophys. Res. Commun. 230, 30-34.
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  31. Friedebold, J., Mayer, F., Bill, E., Trautwein, A.X. and Bowien, B. (1995) Structural and immunological studies on the soluble formate dehydrogenase from Alcaligenes eutrophus. Biol. Chem. Hoppe Seyler 376, 561-568.
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  35. George, G.N. and Bray, R.C. (1988) Studies by electron paramagnetic resonance spectroscopy of xanthine oxidase enriched with molybdenum­95 and with molybdenum­97. Biochemistry 27, 3603-3609.
  36. Gibson, J.F. and Bray, R.C. (1968) Electron spin resonance of non­haem iron in xanthine oxidase. Biochim. Biophys. Acta 153, 721-723.
  37. Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C. (1994) Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium­dependent enzyme. Proc. Natl. Acad. Sci. USA 91, 232-236.
  38. Gladyshev, V.N., Khangulov, S.V. and Stadtman, T.C. (1996) Properties of the selenium­ and molybdenum­containing nicotinic acid hydroxylase from Clostridium barkeri. Biochemistry 35, 212-223.
  39. Gutteridge, S. and Bray, R.C. (1980) Oxygen­17 splitting of the Very Rapid molybdenum(V) e.p.r. signal from xanthine oxidase. Rate of exchange with water of the coupled oxygen atom. Biochem. J. 189, 615-623.
  40. Gutteridge, S., Tanner, S.J. and Bray, R.C. (1978a) The molybdenum centre of native xanthine oxidase. Evidence for proton transfer from substrates to the centre and for existence of an anion­binding site. Biochem. J. 175, 869-878.
  41. Gutteridge, S., Tanner, S.J. and Bray, R.C. (1978b) Comparison of the molybdenum centres of native and desulpho xanthine oxidase. The nature of the cyanide­labile sulphur atom and the nature of the proton­accepting group. Biochem. J. 175, 887-897.
  42. Hänzelmann, P. and Meyer, O. (1998) Effect of molybdate and tungstate on the biosynthesis of CO dehydrogenase and the molybdopterin cytosine­dinucleotide­type of molybdenum cofactor in Hydrogenophaga pseudoflava. Eur. J. Biochem. 255, 755-765.
  43. Hawkes, T.R. and Bray, R.C. (1984) Studies by electron­paramagnetic­resonance spectroscopy of the environment of the metal in the molybdenum cofactor of molybdenum­containing enzymes. Biochem. J. 222, 587-600.
  44. Hawkes, T.R., George, G.N. and Bray, R.C. (1984) The structure of the inhibitory complex of alloxanthine (1H­pyrazolo[3,4­d]pyrimidine­4,6­diol) with the molybdenum centre of xanthine oxidase from electron­paramagnetic­resonance spectroscopy. Biochem. J. 218, 961-968.
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