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Last modified: 9 April 1999

Bibliography on structural studies of P450 proteins

  1. Andersson, L.A. and Peterson, J.A. (1995) Active­site analysis of ferric P450 enzymes: hydrogen­bonding effects on the circular dichroism spectra. Biochem. Biophys. Res. Commun. 211, 389-395.
  2. Andersson, L.A., Sono, M. and Dawson, J.H. (1983) Circular dichroism studies of low­spin ferric cytochrome P­450CAM ligand complexes. Biochim. Biophys. Acta 748, 341-352.
  3. 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.
  4. Anzenbacher, P., Bec, N., Hudecek, J., Lange, R. and Anzenbacherova, E. (1998a) High conformational stability of cytochrome P­450 1A2. Evidence from UV absorption spectra. Collect. Czechoslovak Chem. Commun. 63, 441-448.
  5. Anzenbacher, P., Hudecek, J., Lange, R. and Bancel, F. (1998b) Accessibility of tyrosine residues in cytochrome P­450scc (CYP11A1). Collect. Czechoslovak Chem. Commun. 63, 1678-1682.
  6. Bancel, F., Bec, N., Ebel, C. and Lange, R. (1997) A central role for water in the control of the spin state of cytochrome P­450scc. Eur. J. Biochem. 250, 276-285.
  7. Banci, L., Bertini, I., Marconi, S. and Pierattelli, R. (1993a) 1H­NMR study of reduced heme proteins myoglobin and cytochrome P450. Eur. J. Biochem. 215, 431-437.
  8. Banci, L., Bertini, I., Eltis, L.D. and Pierattelli, R. (1993b) Spectroscopic characterization of a newly isolated cytochrome P450 from Rhodococcus rhodochrous. Biophys. J. 65, 806-813.
  9. Bangcharoenpaurpong, O., Rizos, A.K., Champion, P.M., Jollie, D. and Sligar, S.G. (1986) Resonance Raman detection of bound dioxygen in cytochrome P­450cam. J. Biol. Chem. 261, 8089-8092.
  10. Benson, D.E., Suslick, K.S. and Sligar, S.G. (1997) Reduced oxy intermediate observed in D251N cytochrome P450cam. Biochemistry 36, 5104-5107.
  11. Boddupalli, S.S., Hasemann, C.A., Ravichandran, K.G., Lu, J.Y., Goldsmith, E.J., Deisenhofer, J. and Peterson, J.A. (1992) Crystallization and preliminary x­ray diffraction analysis of P450terp and the hemoprotein domain of P450BM­3, enzymes belonging to two distinct classes of the cytochrome P450 superfamily. Proc. Natl. Acad. Sci. USA 89, 5567-5571.
  12. Champion, P.M., Lipscomb, J.D., Münck, E., Debrunner, P.G. and Gunsalus, I.C. (1975) Mössbauer investigations of high­spin ferrous heme proteins. I. Cytochrome P­450. Biochemistry 14, 4151-4158.
  13. Chevion, M., Peisach, J. and Blumberg, W.E. (1977) Imidazole, the ligand trans to mercaptide in ferric cytochrome P­450. An EPR study of proteins and model compounds. J. Biol. Chem. 252, 3637-3645.
  14. Contzen, J. and Jung, C. (1998) Step­scan time­resolved FTIR spectroscopy of cytochrome P­450cam carbon monoxide complex: A salt link involved in the ligand­rebinding process. Biochemistry 37, 4317-4324.
  15. Contzen, J., Ristau, O. and Jung, C. (1996) Time­resolved Fourier­transform infrared studies of the cytochrome P­450cam carbon monoxide complex bound with (1R)­camphor and (1S)­camphor. FEBS Lett. 383, 13-17.
  16. Crull, G.B., Kennington, J.W., Garber, A.R., Ellis, P.D. and Dawson, J.H. (1989) 19F nuclear magnetic resonance as a probe of the spatial relationship between the heme iron of cytochrome P­450 and its substrate. J. Biol. Chem. 264, 2649-2655.
  17. Cupp­Vickery, J.R. and Poulos, T.L. (1995) Structure of cytochrome P450eryF involved in erythromycin biosynthesis. Nature Struct. Biol. 2, 144-153.
  18. Cupp­Vickery, J.R. and Poulos, T.L. (1997) Structure of cytochrome P450eryF: Substrate, inhibitors, and model compounds bound in the active site. Steroids 62, 112-116.
  19. Cupp­Vickery, J.R., Li, H. and Poulos, T.L. (1994) Preliminary crystallographic analysis of an enzyme involved in erythromycin biosynthesis: cytochrome P450eryF. Proteins 20, 197-201.
  20. Davydov, D.R., Hui Bon Hoa, G. and Peterson, J.A. (1999) Dynamics of protein­bound water in the heme domain of P450BM3 studied by high­pressure spectroscopy: Comparison with P450cam and P450 2B4. Biochemistry 38, 751-761.
  21. Davydov, R.M., Greschner, S. and Ruckpaul, K. (1979) Absorption and magnetic circular dichroism spectra of heme proteins in nonequilibrium states. V. Cytochrome P450 and its substrate complex. Mol. Biol. (Moscow) 13, 1397-1406.
  22. Dawson, J.H., Andersson, L.A. and Sono, M. (1982) Spectroscopic investigations of ferric cytochrome P­450­CAM ligand complexes. Identification of the ligand trans to cysteinate in the native enzyme. J. Biol. Chem. 257, 3606-3617.
  23. Dawson, J.H., Andersson, L.A. and Sono, M. (1983) The diverse spectroscopic properties of ferrous cytochrome P­450­CAM ligand complexes. J. Biol. Chem. 258, 13637-13645.
  24. Deprez, E., Gerber, N.C., Di Primo, C., Douzou, P., Sligar, S.G. and Hui Bon Hoa, G. (1994) Electrostatic control of the substrate access channel in cytochrome P­450cam. Biochemistry 33, 14464-14468.
  25. Di Gleria, K., Nickerson, D.P., Hill, H.A.O., Wong, L.­L. and Fülöp, V. (1998) Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein. J. Am. Chem. Soc. 120, 46-52.
  26. Di Primo, C., Hui Bon Hoa, G., Douzou, P. and Sligar, S.G. (1990) Mutagenesis of a single hydrogen bond in cytochrome P­450 alters cation binding and heme solvation. J. Biol. Chem. 265, 5361-5363.
  27. Di Primo, C., Hui Bon Hoa, G., Douzou, P. and Sligar, S.G. (1992) Heme­pocket­hydration change during the inactivation of cytochrome P­450camphor by hydrostatic pressure. Eur. J. Biochem. 209, 583-588.
  28. Di Primo, C., Deprez, E., Sligar, S.G. and Hui Bon Hoa, G. (1997) Origin of the photoacoustic signal in cytochrome P­450cam: Role of the Arg186-Asp251-Lys178 bifurcated salt bridge. Biochemistry 36, 112-118.
  29. Egawa, T., Ogura, T., Makino, R., Ishimura, Y. and Kitagawa, T. (1991) Observation of the O-O stretching Raman band for cytochrome P­450cam under catalytic conditions. J. Biol. Chem. 266, 10246-10248.
  30. Egawa, T., Shimada, H. and Ishimura, Y. (1994) Evidence for compound I formation in the reaction of cytochrome P450cam with m­chloroperbenzoic acid. Biochem. Biophys. Res. Commun. 201, 1464-1469.
  31. Filipovic, D., Paulsen, M.D., Loida, P.J., Sligar, S.G. and Ornstein, R.L. (1992) Ethylbenzene hydroxylation by cytochrome P450cam. Biochem. Biophys. Res. Commun. 189, 488-495.
  32. Fisher, M.T. and Sligar, S.G. (1987) Temperature jump relaxation kinetics of the P­450cam spin equilibrium. Biochemistry 26, 4797-4803.
  33. Fisher, M.T., Scarlata, S.F. and Sligar, S.G. (1985) High­pressure investigations of cytochrome P­450 spin and substrate binding equilibria. Arch. Biochem. Biophys. 240, 456-463.
  34. Gelb, M.H., Toscano, W.A. and Sligar, S.G. (1982) Chemical mechanisms for cytochrome P­450 oxidation: spectral and catalytic properties of a manganese­substituted protein. Proc. Natl. Acad. Sci. USA 79, 5758-5762.
  35. Goldfarb, D., Bernardo, M., Thomann, H., Kroneck, P.M.H. and Ullrich, V. (1996) Study of water binding to low­spin Fe(III) in cytochrome P450 by pulsed ENDOR and four­pulse ESEEM spectroscopies. J. Am. Chem. Soc. 118, 2686-2693.
  36. Greschner, S., Sharonov, Yu.A. and Jung, C. (1993) Substrate induced changes of the active site electronic states in reduced cytochrome P450cam and the photolysis product of its CO complex. Low­temperature magnetic circular dichroism data. FEBS Lett. 315, 153-158.
  37. Hahn, J.E., Hodgson, K.O., Andersson, L.A. and Dawson, J.H. (1982) Endogenous cysteine ligation in ferric and ferrous cytochrome P­450. Direct evidence from x­ray absorption spectroscopy. J. Biol. Chem. 257, 10934-10941.
  38. Hasemann, C.A., Ravichandran, K.G., Peterson, J.A. and Deisenhofer, J. (1994) Crystal structure and refinement of cytochrome P450terp at 2.3 Å resolution. J. Mol. Biol. 236, 1169-1185.
  39. Helms, V., Deprez, E., Gill, E., Barret, C., Hui Bon Hoa, G. and Wade, R.C. (1996) Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket. Biochemistry 35, 1485-1499.
  40. Hudecek, J., Baumruk, V., Anzenbacher, P. and Munro, A.W. (1998) Catalytically self­sufficient P450 CYP102 (cytochrome P450 BM­3): resonance Raman spectral characterization of the heme domain and of the holoenzyme. Biochem. Biophys. Res. Commun. 243, 811-815.
  41. Jung, C., Hui Bon Hoa, G., Schroder, K.L., Simon, M. and Doucet, J.P. (1992) Substrate analogue induced changes of the CO­stretching mode in the cytochrome P450cam-carbon monoxide complex. Biochemistry 31, 12855-12862.
  42. Jung, C., Hui Bon Hoa, G., Davydov, D., Gill, E. and Heremans, K. (1995) Compressibility of the heme pocket of substrate analogue complexes of cytochrome P­450cam-CO. The effect of hydrostatic pressure on the Soret band. Eur. J. Biochem. 233, 600-606.
  43. Jung, C., Ristau, O., Schulze, H. and Sligar, S.G. (1996a) The CO stretching mode infrared spectrum of substrate­free cytochrome P­450cam-CO. The effect of solvent conditions, temperature, and pressure. Eur. J. Biochem. 235, 660-669.
  44. Jung, C., Schulze, H. and Deprez, E. (1996b) Role of the polarity of the heme environment for the CO stretch modes in cytochrome P­450cam-CO. Biochemistry 35, 15088-15094.
  45. Kadkhodayan, S., Coulter, E.D., Maryniak, D.M., Bryson, T.A. and Dawson, J.H. (1995) Uncoupling oxygen transfer and electron transfer in the oxygenation of camphor analogues by cytochrome P450­CAM. Direct observation of an intermolecular isotope effect for substrate C­H activation. J. Biol. Chem. 270, 28042-28048.
  46. Kobayashi, K., Iwamoto, T. and Honda, K. (1994) Spectral intermediate in the reaction of ferrous cytochrome P450cam with superoxide anion. Biochem. Biophys. Res. Commun. 201, 1348-1355.
  47. Legrand, N., Bondon, A., Simonneaux, G., Jung, C. and Gill, E. (1995) Substrate interactions in cytochrome P­450: correlation between carbon­13 nuclear magnetic resonance chemical shifts and C­O vibrational frequencies. FEBS Lett. 364
  48. Li, H. and Poulos, T.L. (1997) The structure of the cytochrome P450BM­3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nature Struct. Biol. 4, 140-146.
  49. Li, H., Narasimhulu, S., Havran, L.M., Winkler, J.D. and Poulos, T.L. (1995) Crystal structure of cytochrome P450cam complexed with its catalytic product, 5­exo­hydroxycamphor. J. Am. Chem. Soc. 117, 6297-6299.
  50. 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.
  51. Loida, P.G., Sligar, S.G., Paulsen, M.D., Arnold, G.E. and Ornstein, R.L. (1995) Stereoselective hydroxylation of norcamphor by cytochrome P450cam. Experimental verification of molecular dynamics simulations. J. Biol. Chem. 270, 5326-5330.
  52. 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.
  53. Macdonald, I.D.G., Sligar, S.G., Christian, J.F., Unno, M. and Champion, P.M. (1999) Identification of the Fe-O-O bending mode in oxycytochrome P450cam by resonance Raman spectroscopy. J. Am. Chem. Soc. 121, 376-380.
  54. Martinis, S.A., Blanke, S.R., Hager, L.P., Sligar, S.G., Hui Bon Hoa, G., Rux, J.J. and Dawson, J.H. (1996) Probing the heme iron coordination structure of pressure­induced cytochrome P420cam. Biochemistry 35, 14530-14536.
  55. Masuya, F., Tsubaki, M., Makino, R. and Hori, H. (1994) EPR studies on the photoproducts of ferric cytochrome P450cam (CYP101) nitrosyl complexes: Effects of camphor and its analogues on ligand­bound structures. J. Biochem. (Tokyo) 116, 1146-1152.
  56. Mouro, C., Jung, C., Bondon, A. and Simonneaux, G. (1997a) Comparative Fourier transform infrared studies of the secondary structure and the CO heme ligand environment in cytochrome P­450cam and cytochrome P­420cam. Biochemistry 36, 8125-8134.
  57. Mouro, C., Jung, C., Bondon, A. and Simonneaux, G. (1997b) 1H­NMR study of diamagnetic cytochrome P450cam: assignment of heme resonances and substrate dependance of one cysteinate ß proton. FEBS Lett. 414, 203-208.
  58. Nakahara, K., Shoun, H., Adachi, S.­i., Iizuka, T. and Shiro, Y. (1994) Crystallization and preliminary X­ray diffraction studies of nitric oxide reductase cytochrome P450nor from Fusarium oxysporum. J. Mol. Biol. 239, 158-159.
  59. Nakamura, K., Horiuchi, T., Yasukochi, T., Sekimizu, K., Hara, T. and Sagara, Y. (1994) Significant contribution of arginine­112 and its positive charge of Pseudomonas putida cytochrome P­450cam in the electron transport from putidaredoxin. Biochim. Biophys. Acta 1207, 40-48.
  60. Nickerson, D., Wong, L.­L. and Rao, Z. (1998) An improved procedure for the preparation of X­ray diffraction­quality crystals of cytochrome P450cam. Acta Crystallogr. D54, 470-472.
  61. Noble, M.A., Quaroni, L., Chumanov, G.D., Turner, K.L., Chapman, S.K., Hanzlik, R.P. and Munro, A.W. (1998) Imidazolyl carboxylic acids as mechanistic probes of flavocytochrome P­450 BM3. Biochemistry 37, 15799-15807.
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Reviews on P450s