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Bibliography on structural studies of sulphite oxidase family

  1. Barber, M.J. and Kay, C.J. (1996) Superoxide production during reduction of molecular oxygen by assimilatory nitrate reductase. Arch. Biochem. Biophys. 326, 227-232.
  2. Barber, M.J. and Solomonson, L.P. (1986) The role of the essential sulfhydryl group in assimilatory NADH:nitrate reductase of Chlorella. J. Biol. Chem. 261, 4562-4567.
  3. Barber, M.J., Notton, B.A. and Solomonson, L.P. (1987) Oxidation­reduction midpoint potentials of the molybdenum center in spinach NADH:nitrate reductase. FEBS Lett. 213, 372-374.
  4. Bray, R.C., Lamy, M.T., Gutteridge, S. and Wilkinson, T. (1982) Evidence from electron­paramagnetic­resonance spectroscopy for a complex of sulphite ions with the molybdenum centre of sulphite oxidase. Biochem. J. 201, 241-243.
  5. Bray, R.C., Gutteridge, S., Lamy, M.T. and Wilkinson, T. (1983) Equilibria amongst different molybdenum(V)­containing species from sulphite oxidase. Evidence for a halide ligand of molybdenum in the low­pH species. Biochem. J. 211, 227-236.
  6. Cohen, H.J., Betcher­Lange, S., Kessler, D.L. and Rajagopalan, K.V. (1972) Hepatic sulfite oxidase. Congruency in mitochondria of prosthetic groups and activity. J. Biol. Chem. 247, 7759-7766.
  7. Coughlan, M.P., Johnson, J.L. and Rajagopalan, K.V. (1980) Mechanisms of inactivation of molybdoenzymes by cyanide. J. Biol. Chem. 255, 2694-2699.
  8. Cramer, S.P., Johnson, J.L., Rajagopalan, K.V. and Sorrell, T.N. (1979) Observation of 17O effects on MoV EPR spectra in sulfite oxidase, xanthine dehydrogenase, and MoO(SC6H5)4-. Biochem. Biophys. Res. Commun. 91, 434-439.
  9. Fukuoka, M., Fukumori, Y. and Yamanaka, T. (1987) Nitrobacter winogradskyi cytochrome a1c1 is an iron-sulfur molybdoenzyme having hemes a and c. J. Biochem. (Tokyo) 102, 525-530.
  10. Gardlik, S. and Rajagopalan, K.V. (1990) The state of reduction of molybdopterin in xanthine oxidase and sulfite oxidase. J. Biol. Chem. 265, 13047-13054.
  11. Garton, S.G., Garrett, R.M., Rajagopalan, K.V. and Johnson, M.K. (1997) Resonance Raman characterization of the molybdenum center in sulfite oxidase: Identification of Mo=O stretching modes. J. Am. Chem. Soc. 119, 2590-2591.
  12. George, G.N., Prince, R.C., Kipke, C.A., Sunde, R.A. and Enemark, J.H. (1988) The nature of the phosphate complex of sulphite oxidase from electron­paramagnetic­resonance studies. Biochem. J. 256, 307-309.
  13. George, G.N., Kipke, C.A., Prince, R.C., Sunde, R.A., Enemark, J.H. and Cramer, S.P. (1989) Structure of the active site of sulfite oxidase. X­ray absorption spectroscopy of the Mo(IV), Mo(V), and Mo(VI) oxidation states. Biochemistry 28, 5075-5080.
  14. George, G.N., Garrett, R.M., Prince, R.C. and Rajagopalan, K.V. (1996) The molybdenum site of sulfite oxidase: A comparison of wild­type and the cysteine 207 to serine mutant using X­ray absorption spectroscopy. J. Am. Chem. Soc. 118, 8588-8592.
  15. George, G.N., Garrett, R.M., Graf, T., Prince, R.C. and Rajagopalan, K.V. (1998) Interaction of arsenate with the molybdenum site of sulfite oxidase. J. Am. Chem. Soc. 120, 4522-4523.
  16. Guiard, B. and Lederer, F. (1977) The "b5­like" domain from chicken­liver sulfite oxidase: A new case of common ancestral origin with liver cytochrome b5 and bakers' yeast cytochrome b2 core. Eur. J. Biochem. 74, 181-190.
  17. Gutteridge, S., Lamy, M.T. and Bray, R.C. (1980) The nature of the phosphate inhibitor complex of sulphite oxidase from electron­paramagnetic­resonance studies using oxygen­17. Biochem. J. 191, 285-288.
  18. Gutteridge, S., Bray, R.C., Notton, B.A., Fido, R.J. and Hewitt, E.J. (1983) Studies by electron­paramagnetic­resonance spectroscopy of the molybdenum centre of spinach (Spinacia oleracea) nitrate reductase. Biochem. J. 213, 137-142.
  19. Johnson, J.L. and Rajagopalan, K.V. (1976) Electron paramagnetic resonance of the tungsten derivative of rat liver sulfite oxidase. J. Biol. Chem. 251, 5505-5511.
  20. Johnson, J.L. and Rajagopalan, K.V. (1977) Tryptic cleavage of rat liver sulfite oxidase. Isolation and characterization of molybdenum and heme domains. J. Biol. Chem. 252, 2017-2025.
  21. Johnson, J.L., Rajagopalan, K.V. and Cohen, H.J. (1974a) Molecular basis of the biological function of molybdenum. Effect of tungsten on xanthine oxidase and sulfite oxidase in the rat. J. Biol. Chem. 249, 859-866.
  22. Johnson, J.L., Cohen, H.J. and Rajagopalan, K.V. (1974b) Molecular basis of the biological function of molybdenum. Molybdenum­free sulfite oxidase from livers of tungsten­treated rats. J. Biol. Chem. 249, 5046-5055.
  23. Johnson, J.L., Hainline, B.E. and Rajagopalan, K.V. (1980) Characterization of the molybdenum cofactor of sulfite oxidase, xanthine oxidase, and nitrate reductase. Identification of a pteridine as a structural component. J. Biol. Chem. 255, 1783-1786.
  24. Johnson, J.L., Hainline, B.E., Rajagopalan, K.V. and Arison, B.H. (1984) The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J. Biol. Chem. 259, 5414-5422.
  25. Kay, C.J. and Barber, M.J. (1989) EPR and kinetic analysis of the interaction of halides and phosphate with nitrate reductase. Biochemistry 28, 5750-5758.
  26. Kay, C.J., Barber, M.J. and Solomonson, L.P. (1988) Circular dichroism and potentiometry of FAD, heme and Mo­pterin prosthetic groups of assimilatory nitrate reductase. Biochemistry 27, 6142-6149.
  27. Kay, C.J., Solomonson, L.P. and Barber, M.J. (1990) Oxidation­reduction potentials of flavin and Mo­pterin centers in assimilatory nitrate reductase: Variation with pH. Biochemistry 29, 10823-10828.
  28. Kessler, D.L. and Rajagopalan, K.V. (1972) Purification and properties of sulfite oxidase from chicken liver. Presence of molybdenum in sulfite oxidase from diverse sources. J. Biol. Chem. 247, 6566-6573.
  29. Kessler, D.L. and Rajagopalan, K.V. (1974a) Hepatic sulfite oxidase. Effect of anions on interaction with cytochrome c. Biochim. Biophys. Acta 370, 389-398.
  30. Kessler, D.L. and Rajagopalan, K.V. (1974b) Hepatic sulfite oxidase. Identification of the molybdenum center as the site of irreversible inactivation by ferricyanide. Biochim. Biophys. Acta 370, 399-409.
  31. Kisker, C., Schindelin, H., Pacheco, A., Wehbi, W.A., Garrett, R.M., Rajagopalan, K.V., Enemark, J.H. and Rees, D.C. (1997) Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase. Cell 91, 973-983.
  32. Kramer, S.P., Johnson, J.L., Ribeiro, A.A., Millington, D.S. and Rajagopalan, K.V. (1987) The structure of the molybdenum cofactor. Characterization of di­(carboxamidomethyl)molybdopterin from sulfite oxidase and xanthine oxidase. J. Biol. Chem. 262, 16357-16363.
  33. Lamy, M.T., Gutteridge, S. and Bray, R.C. (1980) Electron­paramagnetic­resonance parameters of molybdenum(V) in sulphite oxidase from chicken liver. Biochem. J. 185, 397-403.
  34. Lu, G., Campbell, W.H., Lindqvist, Y. and Schneider, G. (1992) Crystallization and preliminary crystallographic studies of the FAD domain of corn NADH:nitrate reductase. J. Mol. Biol. 224, 277-279.
  35. Lu, G., Campbell, W.H., Schneider, G. and Lindqvist, Y. (1994) Crystal structure of the FAD­containing fragment of corn nitrate reductase at 2.5 Å resolution: Relationship to other flavoprotein reductases. Structure 2, 809-821.
  36. Lu, G., Lindqvist, Y. and Schneider, G. (1995a) A method for processing diffraction data from twinned protein crystals and its application in the structure determination of an FAD/NADH­binding fragment of nitrate reductase. Acta Crystallogr. D51, 13-20.
  37. Lu, G., Lindqvist, Y., Schneider, G., Dwivedi, U. and Campbell, W.H. (1995b) Structural studies on corn nitrate reductase: refined structure of the cytochrome b reductase fragment at 2.5 Å, its ADP complex and an active­site mutant and modeling of the cytochrome b domain. J. Mol. Biol. 248, 931-948.
  38. Onoue, Y. (1980) Sulfite oxidase from Merluccius productus. Biochim. Biophys. Acta 615, 48-58.
  39. Quinn, G.B., Trimboli, A.J., Prosser, I.M. and Barber, M.J. (1996) Spectroscopic and kinetic properties of a recombinant form of the flavin domain of spinach NADH:nitrate reductase. Arch. Biochem. Biophys. 327, 151-160.
  40. Raitsimring, A.M., Pacheco, A. and Enemark, J.H. (1998) ESEEM investigations of the high pH and low pH forms of chicken liver sulfite oxidase. J. Am. Chem. Soc. 120, 11263-11278.
  41. Ratnam, K., Shiraishi, N., Campbell, W.H. and Hille, R. (1997) Spectroscopic and kinetic characterization of the recombinant cytochrome c reductase fragment of nitrate reductase. Identification of the rate­limiting catalytic step. J. Biol. Chem. 272, 2122-2128.
  42. Solomonson, L.P., Barber, M.J., Howard, W.D., Johnson, J.L. and Rajagopalan, K.V. (1984) Electron paramagnetic resonance studies on the molybdenum center of assimilatory NADH:nitrate reductase from Chlorella vulgaris. J. Biol. Chem. 259, 849-853.
  43. Solomonson, L.P., Barber, M.J., Robbins, A.P. and Oaks, A. (1986) Functional domains of assimilatory NADH:nitrate reductase from Chlorella. J. Biol. Chem. 261, 11290-11294.
  44. Toghrol, F. and Southerland, W.M. (1983) Purification of Thiobacillus novellus sulfite oxidase. Evidence for the presence of heme and molybdenum. J. Biol. Chem. 258, 6762-6766.