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Bibliography on structural studies of haem chloroperoxidase

  1. Andersson, L.A., Johnson, A.K. and Peterson, J.A. (1997) Active site analysis of P450 enzymes: comparative magnetic circular dichroism spectroscopy. Arch. Biochem. Biophys. 345, 79-87.
  2. Bangcharoenpaurpong, O., Champion, P.M., Hall, K.S. and Hager, L.P. (1986) Resonance Raman studies of isotopically labeled chloroperoxidase. Biochemistry 25, 2374-2378.
  3. 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.
  4. 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.
  5. Blanke, S.R., Martinis, S.A., Sligar, S.G., Hager, L.P., Rux, J.J. and Dawson, J.H. (1996) Probing the heme iron coordination structure of alkaline chloroperoxidase. Biochemistry 35, 14537-14543.
  6. Casella, L., Gullotti, M., Ghezzi, R., Poli, S., Beringhelli, T., Colonna, S. and Carrea, G. (1992) Mechanism of enantioselective oxygenation of sulfides catalyzed by chloroperoxidase and horseradish peroxidase. Spectral studies and characterization of enzyme-substrate complexes. Biochemistry 31, 9451-9459.
  7. Champion, P.M., Münck, E., Debrunner, P.G., Hollenberg, P.F. and Hager, L.P. (1973) Mössbauer investigations of chloroperoxidase and its halide complexes. Biochemistry 12, 426-435.
  8. Champion, P.M., Chiang, R., Münck, E., Debrunner, P.G. and Hager, L.P. (1975) Mössbauer investigations of high­spin ferrous heme proteins. II. Chloroperoxidase, horseradish peroxidase, and hemoglobin. Biochemistry 14, 4159-4166.
  9. Champion, P.M., Remba, R.D., Chiang, R., Fitchen, D.B. and Hager, L.P. (1976) Resonance Raman spectra of chloroperoxidase. Biochim. Biophys. Acta 446, 486-492.
  10. Chiang, R., Makino, R., Spomer, W.E. and Hager, L.P. (1975) Chloroperoxidase: P­450 type absorption in the absence of sulfhydryl groups. Biochemistry 14, 4166-4171.
  11. Cramer, S.P., Dawson, J.H., Hodgson, K.O. and Hager, L.P. (1978) Studies on the ferric forms of cytochrome P450 and chloroperoxidase by extended X­ray absorption fine structure. Characterization of the Fe-N and Fe-S distance. J. Am. Chem. Soc. 100, 7282-7290.
  12. Debrunner, P.G., Dexter, A.F., Schulz, C.E., Xia, Y.­M. and Hager, L.P. (1996) Mössbauer and electron paramagnetic resonance studies of chloroperoxidase following mechanism­based inactivation with allylbenzene. Proc. Natl. Acad. Sci. USA 93, 12791-12798.
  13. Dugad, L.B., Wang, X., Wang, C.C., Lukat, G.S. and Goff, H.M. (1992) Proton nuclear Overhauser effect study of the heme active site structure of chloroperoxidase. Biochemistry 31, 1651-1655.
  14. Egawa, T., Miki, H., Ogura, T., Makino, R., Ishimura, Y. and Kitagawa, T. (1992) Observation of the FeIV=O stretching Raman band for a thiolate­ligated heme protein. Compound I of chloroperoxidase. FEBS Lett. 305, 206-208.
  15. Goff, H.M., Gonzalez­Vergara, E. and Bird, M.R. (1985) High­resolution proton nuclear magnetic resonance spectroscopy of chloride peroxidase: identification of new forms of the enzyme. Biochemistry 24, 1007-1013.
  16. Hollenberg, P.F., Hager, L.P., Blumberg, W.E. and Peisach, J. (1980) An electron paramagnetic resonance study of the high and low spin forms of chloroperoxidase. J. Biol. Chem. 255, 4801-4807.
  17. Hosten, C.M., Sullivan, A.M., Palaniappan, V., Fitzgerald, M.M. and Terner, J. (1994) Resonance Raman spectroscopy of the catalytic intermediates and derivatives of chloroperoxidase from Caldariomyces fumago. J. Biol. Chem. 269, 13966-13978.
  18. Hu, S. and Kincaid, J.R. (1993) Heme active­site structural characterization of chloroperoxidase by resonance Raman spectroscopy. J. Biol. Chem. 268, 6189-6193.
  19. Krejcarek, G.E., Bryant, R.G., Smith, R.J. and Hager, L.P. (1976) Broad­line nuclear magnetic resonance studies of chloroperoxidase. Biochemistry 15, 2508-2511.
  20. Lee, H.C., Cummings, K., Hall, K., Hager, L.P. and Oldfield, E. (1988) Oxygen­17 nuclear magnetic resonance spectroscopic studies of carbonmonoxyperoxidases. J. Biol. Chem. 263, 16118-16124.
  21. Lee, H.­I., Dexter, A.F., Fann, Y.­C., Lakner, F.J., Hager, L.P. and Hoffman, B.M. (1997) Structure of the modified heme in allylbenzene­inactivated chloroperoxidase determined by Q­band CW and pulsed ENDOR. J. Am. Chem. Soc. 119, 4059-4069.
  22. Liu, H.I., Sono, M., Kadkhodayan, S., Hager, L.P., Hedman, B., Hodgson, K.O. and Dawson, J.H. (1995) X­ray absorption near edge studies of cytochrome P­450­CAM, chloroperoxidase, and myoglobin. Direct evidence for the electron releasing character of a cysteine thiolate proximal ligand. J. Biol. Chem. 270, 10544-10550.
  23. Lukat, G.S. and Goff, H.M. (1986) Proton and nitrogen­15 NMR spectroscopic studies of hydrogen ion­dependent pseudo­halide ion binding to chloroperoxidase. J. Biol. Chem. 261, 16528-16534.
  24. Lukat, G.S. and Goff, H.M. (1990) A nuclear magnetic resonance study of axial ligation for the reduced states of chloroperoxidase, cytochrome P­450cam, and porphinatoiron(II) thiolate complexes. Biochim. Biophys. Acta 1037, 351-359.
  25. Park, K.D., Guo, K.M., Adebodun, F., Chiu, M.L., Sligar, S.G. and Oldfield, E. (1991) Distal and proximal ligand interactions in heme proteins: correlations between C-O and Fe-C vibrational frequencies, oxygen­17 and carbon­13 nuclear magnetic resonance chemical shifts, and oxygen­17 nuclear quadrupole coupling constants in C17O­ and 13CO­labeled species. Biochemistry 30, 2333-2347.
  26. Remba, R.D., Champion, P.M., Fitchen, D.B., Chiang, R. and Hager, L.P. (1979) Resonance Raman investigations of chloroperoxidase, horseradish peroxidase, and cytochrome c using Soret band laser excitation. Biochemistry 18, 2280-2290.
  27. Rubin, B., VanMiddlesworth, J., Thomas, K. and Hager, L.P. (1982) Crystallization and preliminary X­ray data for chloroperoxidase. J. Biol. Chem. 257, 7768-7769.
  28. Rutter, R. and Hager, L.P. (1982) The detection of two electron paramagnetic resonance radical signals associated with chloroperoxidase compound I. J. Biol. Chem. 257, 7958-7961.
  29. Rutter, R., Hager, L.P., Dhonau, H., Hendrich, M., Valentine, M. and Debrunner, P.G. (1984) Chloroperoxidase compound I: Electron paramagnetic resonance and Mössbauer studies. Biochemistry 23, 6809-6816.
  30. Samokyszyn, V.M. and Ortiz de Montellano, P.R. (1991) Topology of the chloroperoxidase active site: regiospecificity of heme modification by phenylhydrazine and sodium azide. Biochemistry 30, 11646-11653.
  31. Sono, M., Dawson, J.H. and Hager, L.P. (1984) The generation of a hyperporphyrin spectrum upon thiol binding to ferric chloroperoxidase. Further evidence of endogenous thiolate ligation to the ferric enzyme. J. Biol. Chem. 259, 13209-13216.
  32. Sono, M., Eble, K.S, Dawson, J.H. and Hager, L.P. (1985) Preparation and properties of ferrous chloroperoxidase complexes with dioxygen, nitric oxide, and an alkyl isocyanide. Spectroscopic dissimilarities between the oxygenated forms of chloroperoxidase and cytochrome P­450. J. Biol. Chem. 260, 15530-15535.
  33. Sono, M., Dawson, J.H., Hall, K. and Hager, L.P. (1986) Ligand and halide binding properties of chloroperoxidase: peroxidase­type active site heme environment with cytochrome P­450 type endogenous axial ligand and spectroscopic properties. Biochemistry 25, 347-356.
  34. Sono, M., Hager, L.P. and Dawson, J.H. (1991) Electron paramagnetic resonance investigations of exogenous ligand complexes of low­spin ferric chloroperoxidase: further support for endogenous thiolate ligation to the heme iron. Biochim. Biophys. Acta 1078, 351-359.
  35. Sundaramoorthy, M., Mauro, J.M., Sullivan, A.M., Terner, J. and Poulos, T.L. (1995a) Preliminary crystallographic analysis of chloroperoxidase from Caldariomyces fumago. Acta Crystallogr. D51, 842-844.
  36. Sundaramoorthy, M., Terner, J. and Poulos, T.L. (1995b) The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure 3, 1367-1378.
  37. Sundaramoorthy, M., Terner, J. and Poulos, T.L. (1998) Stereochemistry of the chloroperoxidase active site: crystallographic and molecular­modeling studies. Chemistry & Biology 5, 461-473.
  38. Wagenknecht, H.­A. and Woggon, W.­D. (1997) Identification of intermediates in the catalytic cycle of chloroperoxidase. Chemistry & Biology 4, 367-372.
  39. Wang, X. and Goff, H.M. (1997) A nuclear paramagnetic relaxation study of the interaction of the cyclopentanedione substrate with chloroperoxidase. Biochim. Biophys. Acta 1339, 88-96.
  40. Yarmola, E.G. and Sharonov, Yu.A. (1994) Low­temperature magnetic circular dichroism investigation of the active site of chloroperoxidase. FEBS Lett. 355, 279-281.
Reviews on haem chloroperoxidase