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Bibliography on structural studies of purple acid phosphatase

  1. Antanaitis, B.C. and Aisen, P. (1982a) EPR signal, purple color, and iron binding in porcine uteroferrin. J. Biol. Chem. 257, 1855-1859.
  2. Antanaitis, B.C. and Aisen, P. (1982b) Detection of a g'=1.74 EPR signal in bovine spleen purple acid phosphatase. J. Biol. Chem. 257, 5330-5332.
  3. Antanaitis, B.C. and Aisen, P. (1985) Effects of perturbants on the pink (reduced) active form of uteroferrin. Phosphate­induced anaerobic oxidation. J. Biol. Chem. 260, 751-756.
  4. Antanaitis, B.C., Aisen, P., Lilienthal, H.R., Roberts, R.M., and Bazer, F.W. (1980) The novel "g'=1.74" EPR spectrum of pink and purple uteroferrin. J. Biol. Chem. 255, 11204-11209.
  5. Antanaitis, B.C., Strekas, T. and Aisen, P. (1982) Characterization of pink and purple uteroferrin by resonance Raman and CD spectroscopy. J. Biol. Chem. 257, 3766-3770.
  6. Antanaitis, B.C., Aisen, P. and Lilienthal, H.R. (1983) Physical characterization of two­iron uteroferrin. Evidence for a spin­coupled binuclear iron cluster. J. Biol. Chem. 258, 3166-3172.
  7. Antanaitis, B.C., Peisach, J., Mims, W.B. and Aisen, P. (1985) Linear electric field effect and electron spin­echo studies of uteroferrin. Evidence for iron coordination by a nitrogen­containing ligand. J. Biol. Chem. 260, 4572-4574.
  8. Battistuzzi, G., Dietrich, M., Löcke, R. and Witzel, H. (1997) Evidence for a conserved binding motif of the dinuclear metal site in mammalian and plant purple acid phosphatases: 1H NMR studies of the di­iron derivative of the Fe(III)Zn(II) enzyme from kidney bean. Biochem. J. 323, 593-596.
  9. Baumbach, G.A., Ketcham, C.M., Richardson, D.E., Bazer, F.W. and Roberts, R.M. (1986) Isolation and characterization of a high molecular weight stable pink form of uteroferrin from uterine secretions and allantoic fluid of pigs. J. Biol. Chem. 261, 12869-12878.
  10. Cashikar, A.G. and Rao, N.M. (1996a) Unfolding pathway in red kidney bean acid phosphatase is dependent on ligand binding. J. Biol. Chem. 271, 4741-4746.
  11. Cashikar, A.G. and Rao, N.M. (1995) Unique structural features of red kidney bean purple acid phosphatase. Indian J. Biochem. Biophys. 32, 130-136.
  12. Cashikar, A.G. and Rao, N.M. (1996b) Role of the intersubunit disulfide bond in the unfolding pathway of dimeric red kidney bean purple acid phosphatase. Biochim. Biophys. Acta 1296, 76-84.
  13. Crans, D.C., Simone, C.M., Holz, R.C. and Que, L., Jr. (1992) Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation. Biochemistry 31, 11731-11739.
  14. Crowder, M.W., Vincent, J.B. and Averill, B.A. (1992) Electron paramagnetic resonance studies on the high­salt form of bovine spleen purple acid phosphatase. Biochemistry 31, 9603-9608.
  15. Davis, J.C. and Averill, B.A. (1982) Evidence for a spin­coupled binuclear iron unit at the active site of the purple acid phosphatase from beef spleen. Proc. Natl. Acad. Sci. USA 79, 4623-4627.
  16. Davis, J.C., Lin, S.S. and Averill, B.A. (1981) Kinetics and optical spectroscopic studies on the purple acid phosphatase from beef spleen. Biochemistry 20, 4062-4067.
  17. Day, E.P., David, S.S., Peterson, J., Dunham, W.R., Bonvoisin, J.J., Sands, R.H. and Que, L., Jr. (1988) Magnetization and electron paramagnetic resonance studies of reduced uteroferrin and its "EPR­silent" phosphate complex. J. Biol. Chem. 263, 15561-15567.
  18. Debrunner, P.G., Hendrich, M.P., de Jersey, J., Keough, D.T., Sage, J.T. and Zerner, B. (1983) Mössbauer and EPR study of the binuclear iron centre in purple acid phosphatase. Biochim. Biophys. Acta 745, 103-106.
  19. Dietrich, M., Münstermann, D., Suerbaum, H. and Witzel, H. (1991) Purple acid phosphatase from bovine spleen. Interactions at the active site in relation to the reaction mechanism. Eur. J. Biochem. 199, 105-113.
  20. Doi, K., Antanaitis, B.C. and Aisen, P. (1986) Absence of iron transfer from uteroferrin to transferrin. J. Biol. Chem. 261, 14936-14938.
  21. Doi, K., Gupta, R. and Aisen, P. (1987) Spectroscopic studies on the interaction of phosphate with uteroferrin. J. Biol. Chem. 262, 6982-6985.
  22. Doi, K., McCracken, J., Peisach, J. and Aisen, P. (1988) The binding of molybdate to uteroferrin. Hyperfine interactions of the binuclear center with 95Mo, 1H, and 2H. J. Biol. Chem. 263, 5757-5763.
  23. Ek­Rylander, B., Barkhem, T., Ljusberg, J., Öhman, L., Andersson, K.K. and Andersson, G. (1997) Comparative studies of rat recombinant purple acid phosphatase and bone tartrate­resistant acid phosphatase. Biochem. J. 321, 305-311.
  24. Gaber, B.P., Sheridan, J.P., Bazer, F.W. and Roberts, R.M. (1979) Resonance Raman scattering from uteroferrin, the purple glycoprotein of the porcine uterus. J. Biol. Chem. 254, 8340-8342.
  25. Hayman, A.R. and Cox, T.M. (1994) Purple acid phosphatase of the human macrophage and osteoclast. Characterization, molecular properties, and crystallization of the recombinant di­iron­oxo protein secreted by baculovirus­infected insect cells. J. Biol. Chem. 269, 1294-1300.
  26. Klabunde, T., Sträter, N., Fröhlich, R., Witzel, H. and Krebs, B. (1996) Mechanism of Fe(III)­Zn(II) purple acid phosphatase based on crystal structures. J. Mol. Biol. 259, 737-748.
  27. Lauffer, R.B., Antanaitis, B.C., Aisen, P. and Que, L., Jr. (1983) 1H NMR studies of porcine uteroferrin. Magnetic interactions and active site structure. J. Biol. Chem. 258, 14212-14218.
  28. Merkx, M. and Averill, B.A. (1998) The activity of oxidized bovine spleen purple acid phosphatase is due to an Fe(III)Zn(II) `impurity'. Biochemistry 37, 11223-11231.
  29. Orlando, J.L., Zirino, T., Quirk, B.J. and Averill, B.A. (1993) Purification and properties of the native form of the purple acid phosphatase from bovine spleen. Biochemistry 32, 8120-8129.
  30. Pyrz, J.W., Sage, J.T., Debrunner, P.G. and Que, L., Jr. (1986) The interaction of phosphate with uteroferrin. Characterization of a reduced uteroferrin-phosphate complex. J. Biol. Chem. 261, 11015-11020.
  31. Saunders, P.T., Renegar, R.H., Raub, T.J., Baumbach, G.A., Atkinson, P.H., Bazer, F.W. and Roberts, R.M. (1985) The carbohydrate structure of porcine uteroferrin and the role of the high mannose chains in promoting uptake by the reticuloendothelial cells of the fetal liver. J. Biol. Chem. 260, 3658-3665.
  32. Sibille, J.C., Doi, K. and Aisen, P. (1987) Hydroxyl radical formation and iron­binding proteins. Stimulation by the purple acid phosphatases. J. Biol. Chem. 262, 59-62.
  33. Sträter, N., Fröhlich, R., Schiemann, A., Krebs, B., Korner, M., Suerbaum, H. and Witzel, H. (1992) Crystallization and preliminary crystallographic data of purple acid phosphatase from red kidney bean. J. Mol. Biol. 224, 511-513.
  34. Sträter, N., Klabunde, T., Tucker, P., Witzel, H. and Krebs, B. (1995) Crystal structure of a purple acid phosphatase containing a dinuclear Fe(III)­Zn(II) active site. Science 268, 1489-1492.
  35. Suerbaum, H., Körner, M., Witzel, H., Althaus, E., Mosel, B.­D. and Müller­Warmuth, W. (1993) Zn­exchange and Mössbauer studies on the [Fe­Fe] derivatives of the purple acid Fe(III)­Zn(II)­phosphatase from kidney beans. Eur. J. Biochem. 214, 313-321.
  36. Sugiura, Y., Kawabe, H., Tanaka, H., Fujimoto, S. and Ohara, A. (1981) Purification, enzymatic properties, and active site environment of a novel manganese(III)­containing acid phosphatase. J. Biol. Chem. 256, 10664-10670.
  37. Vincent, J.B., Crowder, M.W. and Averill, B.A. (1991) Spectroscopic and kinetics studies of a high­salt­stabilized form of the purple acid phosphatase from bovine spleen. Biochemistry 30, 3025-3034.
  38. Wang, X., Randall, C.R., True, A.E. and Que, L., Jr. (1996) X­ray absorption spectroscopic studies of the FeZn derivative of uteroferrin. Biochemistry 35, 13946-13954.
  39. Wang, X. and Que, L., Jr. (1998) Extended X­ray absorption fine structure studies of the anion complexes of FeZn uteroferrin. Biochemistry 37, 7813-7821.
  40. Wang, Z., Ming, L.J., Que, L., Jr., Vincent, J.B., Crowder, M.W. and Averill, B.A. (1992) 1H NMR and NOE studies of the purple acid phosphatases from porcine uterus and bovine spleen. Biochemistry 31, 5263-5268.
  41. Yang, Y.­S., McCormick, J.M. and Solomon, E.I. (1997) Circular dichroism and magnetic circular dichroism studies of the mixed­valence binuclear non­heme iron active site in uteroferrin and its anion complexes. J. Am. Chem. Soc. 119, 11832-11842.
Reviews on purple acid phosphatase