Stereochemistry of the chloroperoxidase active site: Crystallographic and molecular-modeling studies

Chemistry and Biology

Volumn 5, Issue 9, 1998, Pages 461-473

  Sundaramoorthy, M ^a   Terner, James ^b   Poulos, Thomas L ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b VIRGINIA COMMONWEALTH UNIVERSITY   (United States)

Author keywords

Chloroperoxidase; Crystallography; Cytochrome P450; Molecular dynamics; Peroxidase

Indexed keywords

EID: 0032170496     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(98)90003-5     Document Type: Article

References (35)

1. Griffin, B.W. (1992). Chloroperoxidase: a review. In Peroxidases in Chemistry and Biology. (Everse, J., Everse, K.E. and Grisham, M.B., eds) Vol II, pp. 85-137, CRC Press, Boca Raton, FL, USA.
2. Sundaramoorthy, M., Terner, J. & Poulos, T.L. (1995). The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid. Structure 3, 1367-1377.
3. Finzel, B.C, Poulos, T.L. & Kraut, J. (1984). Crystal structure of yeast cytochrome c peroxidase refined at 1.7 Å resolution. J. Biol. Chem. 259, 13027-13036.
4. Poulos, T.L., Cupp-Vickery, J.R. & Li, H. (1995). Structural studies on prokaryotic cytochromes P450. In Cytochrome P450: Structure, Mechanism, and Biochemistry (Ortiz de Montellano, P.R. ed) pp.125-150. Plenum Press, New York.
5. Allain, E.J., Hager, L.P., Deng, L. & Jacobsen, E.N. (1993). Highly selective enantioselective epoxidation of disubstituted alkenes with hydrogen peroxide catalyzed by chloroperoxidase. J. Am. Chem. Soc. 115, 4415-4416.
6. Colonna, S., et al., & Pasta, P. (1990). Enantioselective oxidations of sulfides catalyzed by chloroperoxidase. Biochemistry, 29, 10465-10468.
7. Edwards, S.L. & Poulos, T.L. (1990). Ligand binding and structural perturbations in cytochrome c peroxidase. J. Biol. Chem. 265, 2588-2595.
8. Fukuyama, K., Kunishima, N., Amada, F., Kubota, T. & Matsubara, H. (1995). Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis. J. Biol. Chem. 270, 21884-92.
9. Raag, R. & Poulos, T.L. (1989). Crystal structure of the carbon monoxide-substrate-cytochrome P450CAM ternary complex. Biochemistry 28, 7586-7592.
10. Conti, E., et al., & Bolognesi, M. (1993). X-ray crystal structure of ferric Aplysia limacina myoglobin in different liganded states. J. Mol. Biol. 233, 498-508.
11. Sono, M., Dawson, J.H., Hall, K. & Hager, L.P. (1986). Ligand and halide binding properties of chloroperoxidase: peroxidase-type active site heme environment with cytochrome P-450 type endogenous axial ligand and spectroscopic properties. Biochemistry 25, 347-356.
12. Edwards, S.L., Xuong, N-h., Hamlin, R.C. & Kraut, J. (1987). Crystal structure of cytochrome c peroxidase compound I. Biochemistry 26, 1503-1511.
13. Fulop, V., et al., & Edwards, S.L. (1994). Laue diffraction study on the structure of cytochrome c peroxidase compound I. Structure 2, 201-208.
14. Wagenknecht, H-A. & Woggon, W-D. (1997). Identification of intermediates in the catalytic cycle of chloroperoxidase. Chem. Biol. 4, 367-372.
15. Thomas, J.A., Morris, D.R. & Hager, L.P. (1970). Chloroperoxidase. VIII. Formation of peroxide and halide complexes and their relation to the mechanism of the halogenation reaction. J. Biol. Chem. 245, 3135-3142.
16. Hewson, W.D. & Hager, L.P. (1979). Peroxidases, catalases, and chloroperoxidase. In The Porphyrins, Part B, (Dolphin, D. ed). Vol. 7, pp. 295-332.
17. Roberts, J.E., Hoffman, B.M., Rutter, R., & Hager, L.P. (1981). Electron-nuclear double resonance of horseradish peroxidase compound I. Detection of the porphyrin pi-cation radical. J. Biol. Chem. 256, 2118-2121.
18. Poulos, T.L. & Kraut, J. (1980). The stereochemistry of peroxidase catalysis. J. Biol. Chem. 255, 8199-8205.
19. Araiso, T., Rutter, R., Palcic, M.M., Hager, L.P. & Dunford, H.B. (1980). Kinetic analysis of compound I formation and the catalatic activity of chloroperoxidase. Can. J. Biochem. 59, 233-236.
20. Libby, R.D., Thomas, J.A., Kaiser, L.W. & Hager, L.P. (1981). Chloroperoxidase halogenation reactions. J. Biol. Chem. 257, 5030-5037.
21. Geigert, J., Neidleman, S.L. & Dalietos, D.J. (1983). Novel haloperoxidase substrates: alkynes and cyclopropanes. J. Biol. Chem. 258, 2273-2277.
22. Griffin, B.W. (1983). Mechanism of halide simulated activity of chloroperoxidase. Evidence of enzymatic formation of free hypohalous acid. Biochem. Biophys. Res. Commun. 116, 873-879.
23. Hayashi, Y. & Yamazaki, I. (1979). The oxidation-reduction of compound I/compound II and compound II/ferric couples of horseradish peroxidases A2 and C. J. Biol. Chem. 254, 9101-9106.
24. Fruetel, J.A., Collins, J.R., Camper, D.L., Loew, G.H., Ortiz de Montellano, P.R. (1992). Calculated and experimental asbolute stereochemistry of the styrene and β-methylsytrene epoxides formed by cytochrome P450cam. J. Am. Chem. Soc. 114, 6987-6993.
25. Collins, J.R., Camper, D.L. & Loew, G.H. (1991). Valproic acid metabolism by cytochrome P450: a theoretical study of stereoelectronic modulators of product distribution. J. Am. Chem. Soc. 113, 2736-2743.
26. Blanke, S.R., Yi, S. & Hager, L.P. (1989). Developement of semicontinuous and continuous flow bioreactors for the high level production of chloroperoxidase. Biotechnol. Lett. 11, 842-844.
27. Sundaramoorthy, M., Mauro, J.M., Sullivan, A.M., Terner, J. & Poulos, T.L. (1995). Preliminary crystallographic analysis of chloroperoxidase from Caldariomyces fumago. Acta Crystallogr. D 51, 842-844.
28. Stura, E.A. & Wilson, I.A. (1991). Applications of the streak seeding technique in protein crystallization. J. Cryst. Growth 110, 270-282.
29. Yonetani, T., Yamamoto, H., Erman, J.E., Leigh, J.S., Jr., & Reed, G.H. (1972). Electromagnetic properties of hemoproteins. V. Optical and electron paramagnetic resonance characteristics of nitric oxide derivatives of metalloporphyrin-apohemoprotein complexes. J. Biol. Chem. 247, 2447-2455.
30. David, P.R. (1991). A method for equilibrating protein crystals with heavy-atom reagents. J. Appl. Crystallogr. 24, 1073-1074.
31. Howard, A.J., Gilliland, G.L., Finzel, B.F., Poulos, T.L., Olendorf, D.H. & Salemme, F.R. (1987). The use of an imaging proportional counter in macromolecular crystallography. J. Appl. Crystallogr. 20, 383-387.
32. Otwinowski, Z. & Minor, W, (1996). Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology Vol. 276 Macromolecular Crystallography, Part A. (Carter, C.W., Jr. & Sweet, R.M., eds), pp. 307-326, Academic Press, San Diego, CA, USA.
33. Brünger, A.T. (1992). X-PLOR Manual, Version 3.1: A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
34. Evans, S.V. (1993). SETOR: hardware-lighted three dimensional solid model representation of macromolecules. J. Mol. Graphics 11, 134-138.
35. Kraulis, P.J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structure. J. Appl. Crystallogr. 24, 946-950.