TSRI's main web site PROMISE mirror at TSRI Metalloprotein DB site Created: 3 September 1996
Last modified: 25 February 1999

Bibliography on structural studies of animal haem peroxidases

  1. Behere, D.V., Gonzalez­Vergara, E. and Goff, H.M. (1985a) Comparison of heme environments and proximal ligands in peroxidases and other hemoproteins through carbon­13 nuclear magnetic resonance spectroscopy of carbon monoxide complexes. Biochem. Biophys. Res. Commun. 131, 607-613.
  2. Behere, D.V., Gonzalez­Vergara, E. and Goff, H.M. (1985b) Unique cyanide nitrogen­15 nuclear magnetic resonance chemical shift values for cyano­peroxidase complexes. Relevance to the heme active­site structure and mechanism of peroxide activation. Biochim. Biophys. Acta 832, 319-325.
  3. Chang, C.S., Sinclair, R., Khalid, S., Yamazaki, I., Nakamura, S. and Powers, L. (1993) An extended X­ray absorption fine structure investigation of the structure of the active site of lactoperoxidase. Biochemistry 32, 2780-2786.
  4. Davey, C.A. and Fenna, R.E. (1996) 2.3 Å resolution X­ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: A model for a prereaction complex with hydrogen peroxide. Biochemistry 35, 10967-10973.
  5. Fenna, R.E., Zeng, J. and Davey, C.A. (1995) Structure of the green heme in myeloperoxidase. Arch. Biochem. Biophys. 316, 653-656.
  6. Ferrari, R.P., Traversa, S., De Gioia, L., Fantucci, P., Suriano, G. and Ghibaudi, E.M. (1999) Catechol(amine)s as probes of lactoperoxidase catalytic site structure: spectroscopic and modeling studies. J. Biol. Inorg. Chem. 4, 12-20.
  7. Hu, S., Treat, R.W. and Kincaid, J.R. (1993) Distinct heme active­site structure in lactoperoxidase revealed by resonance Raman spectroscopy. Biochemistry 32, 10125-10130.
  8. Kooter, I.M., Moguilevsky, N., Bollen, A., Sijtsema, N.M., Otto, C. and Wever, R. (1997a) Site­directed mutagenesis of Met243, a residue of myeloperoxidase involved in binding of the prosthetic group. J. Biol. Inorg. Chem. 2, 191-197.
  9. Kooter, I.M., Pierik, A.J., Merkx, M., Averill, B.A., Moguilevsky, N., Bollen, A. and Wever, R. (1997b) Difference Fourier transform infrared evidence for ester bonds linking the heme group in myeloperoxidase, lactoperoxidase, and eosinophil peroxidase. J. Am. Chem. Soc. 119, 11542-11543.
  10. Kulmacz, R.J., Ren, Y., Tsai, A.­L. and Palmer, G. (1990) Prostaglandin H synthase: spectroscopic studies of the interaction with hydroperoxides and with indomethacin. Biochemistry 29, 8760-8771.
  11. Kulmacz, R.J., Palmer, G. and Tsai, A.­L. (1991) Prostaglandin H synthase: perturbation of the tyrosyl radical as a probe of anticyclooxygenase agents. Mol. Pharmacol. 40, 833-837.
  12. Kumar, R., Bhatia, K.L., Dauter, Z., Betzel, C.H. and Singh, T.P. (1995) Purification, crystallization and preliminary X­ray crystallographic analysis of lactoperoxidase from buffalo milk. Acta Crystallogr. D51, 1094-1096.
  13. Kurumbail, R.G., Stevens, A.M., Gierse, J.K., McDonald, J.J., Stegeman, R.A., Pak, J.Y., Gildehaus, D., Miyashiro, J.M., Penning, T.D., Seibert, K., Isakson, P.C. and Stallings, W.C. (1996) Structural basis for selective inhibition of cyclooxygenase­2 by anti­inflammatory agents. Nature 384, 644-648.
  14. Loll, P.J., Picot, D. and Garavito, R.M. (1995) The structural basis of aspirin activity inferred from the crystal structure of inactivated prostaglandin H2 synthase. Nature Struct. Biol. 2, 637-643.
  15. Loll, P.J., Picot, D., Ekabo, O. and Garavito, R.M. (1996) Synthesis and use of iodinated antiinflammatory drug analogs as crystallographic probes of the prostaglandin H2 synthase cyclooxygenase active site. Biochemistry 35, 7330-7340.
  16. López­Garriga, J.J., Oertling, W.A., Kean, R.T., Hoogland, H., Wever, R. and Babcock, G.T. (1990) Metal-ligand vibrations of cyanoferric myeloperoxidase and cyanoferric horseradish peroxidase: evidence for a constrained heme pocket in myeloperoxidase. Biochemistry 29, 9387-9395.
  17. Luong, C., Miller, A., Barnett, J., Chow, J., Ramesha, C. and Browner, M.F. (1996) Flexibility of the NSAID binding site in the structure of human cyclooxygenase­2. Nature Struct. Biol. 3, 927-933.
  18. Manthey, J.A., Boldt, N.J., Bocian, D.F. and Chan, S.I. (1986) Resonance Raman studies of lactoperoxidase. J. Biol. Chem. 261, 6734-6741.
  19. Picot, D., Loll, P.J. and Garavito, R.M. (1994) The X­ray crystal structure of the membrane protein prostaglandin H2 synthase­1. Nature 367, 243-249.
  20. Rae, T.D. and Goff, H.M. (1996) Lactoperoxidase heme structure characterized by paramagnetic proton NMR spectroscopy. J. Am. Chem. Soc. 118, 2103-2104.
  21. Sharonov, Yu.A. (1995) Evidence for the high­spin heme iron in both stable and unstable reduced forms of lactoperoxidase: Low­temperature magnetic circular dichroism data. FEBS Lett. 377, 512-514.
  22. Tsai, A.­L., Kulmacz, R.J., Wang, J.S., Wang, Y., van Wart, H.E. and Palmer, G. (1993) Heme coordination of prostaglandin H synthase. J. Biol. Chem. 268, 8554-8563.
  23. Tsai, A.­L., Kulmacz, R.J. and Palmer, G. (1995) Spectroscopic evidence for reaction of prostaglandin H synthase­1 tyrosyl radical with arachidonic acid. J. Biol. Chem. 270, 10503-10508.
  24. Tsai, A.­L., Wu, G. and Kulmacz, R.J. (1997) Stoichiometry of the interaction of prostaglandin H synthase with substrates. Biochemistry 36, 13085-13094.
  25. Tuynman, A., Vink, M.K.S., Dekker, H.L., Schoemaker, H.E. and Wever, R. (1998) The sulphoxidation of thioanisole catalysed by lactoperoxidase and Coprinus cinereus peroxidase: Evidence for an oxygen­rebound mechanism. Eur. J. Biochem. 258, 906-913.
  26. Xiao, G., Tsai, A.­L., Palmer, G., Boyar, W.C., Marshall, P.J. and Kulmacz, R.J. (1997) Analysis of hydroperoxide­induced tyrosyl radicals and lipoxygenase activity in aspirin­treated human prostaglandin H synthase­2. Biochemistry 36, 1836-1845.
  27. Yue, K.T., Taylor, K.L., Kinkade, J.M., Jr., Sinclair, R.B. and Powers, L.S. (1997) X­ray absorption and resonance Raman spectroscopy of human myeloperoxidase at neutral and acid pH. Biochim. Biophys. Acta 1338, 282-294.
  28. Zeng, J. and Fenna, R.E. (1989) Tetragonal crystals of canine myeloperoxidase suitable for X­ray structural analysis. J. Mol. Biol. 210, 681-683.
  29. Zeng, J. and Fenna, R.E. (1992) X­ray crystal structure of canine myeloperoxidase at 3 Å resolution. J. Mol. Biol. 226, 185-207.
Reviews on animal haem peroxidases