Structural and spectroscopic studies of P450cam

Last modified: Wed Apr 14 12:26:23 BST 2004

• Atkins, W.M. and Sligar, S.G. (1988) The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis. J. Biol. Chem. 263, 18842-18849.
• Bangcharoenpaurpong, O., Rizos, A.K., Champion, P.M., Jollie, D. and Sligar, S.G. (1986) Resonance Raman detection of bound dioxygen in cytochrome P-450cam. J. Biol. Chem. 261, 8089-8092.
• Benson, D.E., Suslick, K.S. and Sligar, S.G. (1997) Reduced oxy intermediate observed in D251N cytochrome P450_cam. Biochemistry 36, 5104-5107.
• Champion, P.M., Lipscomb, J.D., Munck, E., Debrunner, P. and Gunsalus, I.C. (1975) Mössbauer investigations of high-spin ferrous heme proteins. I. Cytochrome P-450. Biochemistry 14, 4151-4158.
• Contzen, J. and Jung, C. (1998) Step-scan time-resolved FTIR spectroscopy of cytochrome P-450_cam carbon monoxide complex: A salt link involved in the ligand-rebinding process. Biochemistry 37, 4317-4324.
• Contzen, J. and Jung, C. (1999) Changes in secondary structure and salt links of cytochrome P-450cam induced by photoreduction: a Fourier transform infrared spectroscopic study. Biochemistry 38, 16253-16260.
• Contzen, J., Ristau, O. and Jung, C. (1996) Time-resolved Fourier-transform infrared studies of the cytochrome P-450cam carbon monoxide complex bound with (1R)-camphor and (1S)-camphor. FEBS Lett. 383, 13-17.
• Contzen, J., Kostka, S., Kraft, R. and Jung, C. (2002) Intermolecular electron transfer in cytochrome P450cam covalently bound with Tris(2,2'-bipyridyl)ruthenium(II): structural changes detected by FTIR spectroscopy. J. Inorg. Biochem. 91, 607-617.
• 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 P-450 and its substrate. J. Biol. Chem. 264, 2649-2655.
• Davydov, R.M., Macdonald, I.D.G., Makris, T.M., Sligar, S.G. and Hoffman, B.M. (1999) EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system. J. Am. Chem. Soc. 121, 10654-10655.
• 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 P-450cam. Biochemistry 33, 14464-14468.
• Deprez, E., Gill, E., Helms, V., Wade, R. and Hui Bon Hoa, G. (2002) Specific and non-specific effects of potassium cations on substrate-protein interactions in cytochromes P450cam and P450lin. J. Inorg. Biochem. 91, 597-606.
• 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 P450_cam as revealed by the crystal structure of the modified protein. J. Am. Chem. Soc. 120, 46-52.
• Di Primo, C., Hui Bon Hoa, G., Douzou, P. and Sligar, S.G. (1990) Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation. J. Biol. Chem. 265, 5361-5363.
• Di Primo, C., Hui Bon Hoa, G., Douzou, P. and Sligar, S.G. (1992) Heme-pocket-hydration change during the inactivation of cytochrome P-450camphor by hydrostatic pressure. Eur. J. Biochem. 209, 583-588.
• Di Primo, C., Deprez, E., Sligar, S.G. and Hui Bon Hoa, G. (1997) Origin of the photoacoustic signal in cytochrome P-450cam: Role of the Arg186-Asp251-Lys178 bifurcated salt bridge. Biochemistry 36, 112-118.
• Egawa, T., Ogura, T., Makino, R., Ishimura, Y. and Kitagawa, T. (1991) Observation of the O-O stretching Raman band for cytochrome P-450cam under catalytic conditions. J. Biol. Chem. 266, 10246-10248.
• Egawa, T., Shimada, H. and Ishimura, Y. (1994) Evidence for compound I formation in the reaction of cytochrome P450cam with m-chloroperbenzoic acid. Biochem. Biophys. Res. Commun. 201, 1464-1469.
• 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.
• Fisher, M.T. and Sligar, S.G. (1987) Temperature jump relaxation kinetics of the P-450cam spin equilibrium. Biochemistry 26, 4797-4803.
• Fisher, M.T., Scarlata, S.F. and Sligar, S.G. (1985) High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria. Arch. Biochem. Biophys. 240, 456-463.
• Gelb, M.H., Toscano, W.A. and Sligar, S.G. (1982) Chemical mechanisms for cytochrome P-450 oxidation: spectral and catalytic properties of a manganese-substituted protein. Proc. Natl. Acad. Sci. USA 79, 5758-5762.
• Gerber, N.C. and Sligar, S.G. (1994) A role for Asp-251 in cytochrome P-450cam oxygen activation. J. Biol. Chem. 269, 4260-4266.
• 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.
• 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. Low-temperature magnetic circular dichroism data. FEBS Lett. 315, 153-158.
• Guallar, V., Baik, M.-H., Lippard, S.J. and Friesner, R.A. (2003) Peripheral heme substituents control the hydrogen-atom abstraction chemistry in cytochromes P450. Proc. Natl. Acad. Sci. USA 100, 6998-7002.
• Hahn, J.E., Hodgson, K.O., Andersson, L.A. and Dawson, J.H. (1982) Endogenous cysteine ligation in ferric and ferrous cytochrome P-450. Direct evidence from x-ray absorption spectroscopy. J. Biol. Chem. 257, 10934-10941.
• 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.
• Hishiki, T., Shimada, H., Nagano, S., Egawa, T., Kanamori, Y., Makino, R., Park, S.-Y., Adachi, S.-i., Shiro, Y. and Ishimura, Y. (2000) X-ray crystal structure and catalytic properties of Thr252Ile mutant of cytochrome P450cam: roles of Thr252 and water in the active center. J. Biochem. (Tokyo) 128, 965-974.
• Jung, C., Hui Bon Hoa, G., Schroder, K.L., Simon, M. and Doucet, J.P. (1992) Substrate analogue induced changes of the CO-stretching mode in the cytochrome P450cam-carbon monoxide complex. Biochemistry 31, 12855-12862.
• 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 P-450cam-CO. The effect of hydrostatic pressure on the Soret band. Eur. J. Biochem. 233, 600-606.
• Jung, C., Ristau, O., Schulze, H. and Sligar, S.G. (1996a) The CO stretching mode infrared spectrum of substrate-free cytochrome P-450cam-CO. The effect of solvent conditions, temperature, and pressure. Eur. J. Biochem. 235, 660-669.
• Jung, C., Schulze, H. and Deprez, E. (1996b) Role of the polarity of the heme environment for the CO stretch modes in cytochrome P-450cam-CO. Biochemistry 35, 15088-15094.
• 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 P450-CAM. Direct observation of an intermolecular isotope effect for substrate C-H activation. J. Biol. Chem. 270, 28042-28048.
• Kimata, Y., Shimada, H., Hirose, T. and Ishimura, Y. (1995) Role of Thr-252 in cytochrome P450cam: a study with unnatural amino acid mutagenesis. Biochem. Biophys. Res. Commun. 208, 96-102.
• 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.
• Legrand, N., Bondon, A., Simonneaux, G., Jung, C. and Gill, E. (1995) Substrate interactions in cytochrome P-450: correlation between carbon-13 nuclear magnetic resonance chemical shifts and C-O vibrational frequencies. FEBS Lett. 364, 152-156.
• Lei, C., Wollenberger, U., Jung, C. and Scheller, F.W. (2000) Clay-bridged electron transfer between cytochrome P450_cam and electrode. Biochem. Biophys. Res. Commun. 268, 740-744.
• Li, H. and Poulos, T.L. (1994) Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures. Structure 2, 461-464.
• 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, 5-exo-hydroxycamphor. J. Am. Chem. Soc. 117, 6297-6299.
• Liu, H.I., Sono, M., Kadkhodayan, S., Hager, L.P., Hedman, B., Hodgson, K.O. and Dawson, J.H. (1995) X-ray absorption near edge studies of cytochrome P-450-CAM, chloroperoxidase, and myoglobin. Direct evidence for the electron releasing character of a cysteine thiolate proximal ligand. J. Biol. Chem. 270, 10544-10550.
• 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.
• 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.
• 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 pressure-induced cytochrome P420cam. Biochemistry 35, 14530-14536.
• 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 ligand-bound structures. J. Biochem. (Tokyo) 116, 1146-1152.
• 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 P-450cam and cytochrome P-420cam. Biochemistry 36, 8125-8134.
• 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.
• Nakamura, K., Horiuchi, T., Yasukochi, T., Sekimizu, K., Hara, T. and Sagara, Y. (1994) Significant contribution of arginine-112 and its positive charge of Pseudomonas putida cytochrome P-450cam in the electron transport from putidaredoxin. Biochim. Biophys. Acta 1207, 40-48.
• Nickerson, D. and Wong, L.-L. (1997) The dimerization of Pseudomonas putida cytochrome P450cam: practical consequences and engineering of a monomeric enzyme. Protein Engineering 10, 1357-1361.
• Nickerson, D., Wong, L.-L. and Rao, Z. (1998) An improved procedure for the preparation of X-ray diffraction-quality crystals of cytochrome P450_cam. Acta Crystallogr. D54, 470-472.
• Nölting, B., Jung, C. and Snatzke, G. (1992) Multichannel circular dichroism investigations of the structural stability of bacterial cytochrome P-450. Biochem. Biophys. Acta 1100, 171-176.
• Pfeil, W., Nölting, B.O. and Jung, C. (1993) Apocytochrome P450cam is a native protein with some intermediate-like properties. Biochemistry 32, 8856-8862.
• Poulos, T.L. (1988) Heme enzyme crystal structures. In Eichhorn, G.L. and Marzilli, L.G., Eds. Advances in Inorganic Biochemistry, vol. 7: Heme Proteins. Elsevier, New York, pp. 1-36.
• Poulos, T.L. (1996) Approaches to crystallizing P450s. Methods Enzymol. 272, 358-368.
• Poulos, T.L. (1991) Modeling of mammalian P450s on basis of P450cam X-ray structure. Methods Enzymol. 206, 11-30.
• Poulos, T.L. and Howard, A.J. (1987) Crystal structures of metyrapone- and phenylimidazole-inhibited complexes of cytochrome P-450cam. Biochemistry 26, 8165-8174.
• Poulos, T.L. and Raag, R. (1992) Cytochrome P450cam: crystallography, oxygen activation, and electron transfer. FASEB J. 6, 674-679.
• Poulos, T.L., Perez, M. and Wagner, G.C. (1982) Preliminary crystallographic data on cytochrome P-450_CAM. J. Biol. Chem. 257, 10427-10429.
• Poulos, T.L., Finzel, B.C., Gunsalus, I.C., Wagner, G.C. and Kraut, J. (1985) The 2.6-Å crystal structure of Pseudomonas putida cytochrome P-450. J. Biol. Chem. 260, 16122-16130.
• Poulos, T.L., Finzel, B.C. and Howard, A.J. (1986) Crystal structure of substrate-free Pseudomonas putida cytochrome P-450. Biochemistry 25, 5314-5322.
• Poulos, T.L., Finzel, B.C. and Howard, A.J. (1987) High-resolution crystal structure of cytochrome P450cam. J. Mol. Biol. 195, 687-700.
• Raag, R. and Poulos, T.L. (1989a) The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450_CAM. Biochemistry 28, 917-922.
• Raag, R. and Poulos, T.L. (1989b) Crystal structure of the carbon monoxide-substrate-cytochrome P-450_CAM ternary complex. Biochemistry 28, 7586-7592.
• Raag, R. and Poulos, T.L. (1991) Crystal structures of cytochrome P-450_CAM complexed with camphane, thiocamphor, and adamantane: factors controlling P-450 substrate hydroxylation. Biochemistry 30, 2674-2684.
• Raag, R., Swanson, B.A., Poulos, T.L. and Ortiz de Montellano, P.R. (1990) Formation, crystal structure, and rearrangement of a cytochrome P-450cam iron-phenyl complex. Biochemistry 29, 8119-8126.
• Raag, R., Martinis, S., Sligar, S.G. and Poulos, T.L. (1991) Crystal structure of the cytochrome P-450cam active site mutant Thr252Ala. Biochemistry 30, 11420-11429.
• Raag, R., Li, H., Jones, B.C. and Poulos, T.L. (1993) Inhibitor-induced conformational change in cytochrome P-450_CAM. Biochemistry 32, 4571-4578.
• Schlichting, I., Jung, C. and Schulze, H. (1997) Crystal structure of cytochrome P­450cam complexed with the (1S)­camphor enantiomer. FEBS Lett. 415, 253-257.
• Schünemann, V., Jung, C., Trautwein, A.X., Mandon, D. and Weiss, R. (2000) Intermediates in the reaction of substrate-free cytochrome P450_cam with peroxy acetic acid. FEBS Lett. 479, 149-154.
• Schünemann, V., Jung, C., Terner, J., Trautwein, A.X. and Weiss, R. (2002) Spectroscopic studies of peroxyacetic acid reaction intermediates of cytochrome P450cam and chloroperoxidase. J. Inorg. Biochem. 91, 586-596.
• Schulze, H., Ristau, O. and Jung, C. (1994a) The proton activity at cryogenic temperatures - a possible influence on the spin state of the heme iron of cytochrome P­450cam in supercooled buffered solutions. Biochim. Biophys. Acta 1183, 491-498.
• Schulze, H., Ristau, O. and Jung, C. (1994b) The carbon monoxide stretching modes in camphor­bound cytochrome P­450cam. The effect of solvent conditions, temperature, and pressure. Eur. J. Biochem. 224, 1047-1055.
• Schulze, H., Hui Bon Hoa, G., Helms, V., Wade, R.C. and Jung, C. (1996) Structural changes in cytochrome P-450_cam effected by the binding of the enantiomers (1R)-camphor and (1S)-camphor. Biochemistry 35, 14127-14138.
• Schulze, H., Hui Bon Hoa, G. and Jung, C. (1997) Mobility of norbornane-type substrates and water accessibility in cytochrome P-450_cam. Biochim. Biophys. Acta 1338, 77-92.
• Sharrock, M., Debrunner, P.G., Schulz, C., Lipscomb, J.D., Marshall, V. and Gunsalus, I.C. (1976) Cytochrome P450cam and its complexes. Mössbauer parameters of the heme iron. Biochim. Biophys. Acta 420, 8-26.
• Shimada, H., Nagano, S., Ariga, Y., Unno, M., Egawa, T., Hishiki, T., Ishimura, Y., Masuya, F., Obata, T. and Hori, H. (1999) Putidaredoxin-cytochrome P450_cam interaction. Spin state of the heme iron modulates putidaredoxin structure. J. Biol. Chem. 274, 9363-9369.
• Stevenson, J.-A., Bearpark, J.K. and Wong, L.-L. (1998) Engineering molecular recognition in alkane oxidation catalysed by cytochrome P450_cam. New J. Chem., 551-552.
• Thomann, H., Goldfarb, D., Bernardo, M., Kroneck, P.M.H. and Ullrich, V. (1995) Evidence for water binding to the Fe center in cytochrome P450cam obtained by ¹⁷O ESEEM, ¹H four-pulse ESEEM and pulsed ENDOR. J. Inorg. Biochem. 59, 322.
• Tetreau, C., Di Primo, C., Lange, R., Tourbez, H. and Lavalette, D. (1997) Dynamics of carbon monoxide binding with cytochromes P-450. Biochemistry 36, 10262-10275.
• Tian, W.D., Wells, A.V., Champion, P.M., Di Primo, C., Gerber, N.C. and Sligar, S.G. (1995) Measurements of CO geminate recombination in cytochromes P450 and P420. J. Biol. Chem. 270, 8673-8679.
• Tschirret-Guth, R.A., Hui Bon Hoa, G. and Ortiz de Montellano, P.R. (1998) Pressure-induced deformation of the cytochrome P450cam active site. J. Am. Chem. Soc. 120, 3590-3596.
• Tuck, S.F., Peterson, J.A. and Ortiz de Montellano, P.R. (1992) Active site topologies of bacterial cytochromes P450101 (P450cam), P450108 (P450terp), and P450102 (P450_BM-3). In situ rearrangement of their phenyl-iron complexes. J. Biol. Chem. 267, 5614-5620.
• Tuck, S.F., Graham-Lorence, S., Peterson, J.A. and Ortiz de Montellano, P.R. (1993) Active sites of the cytochrome P450cam (CYP101) F87W and F87A mutants. Evidence for significant structural reorganization without alteration of catalytic regiospecificity. J. Biol. Chem. 268, 269-275.
• Unno, M., Ishimori, K., Ishimura, Y. and Morishima, I. (1994) High-pressure flash photolysis study of hemoprotein: Effects of substrate analogues on the recombination of carbon monoxide to cytochrome P450_CAM. Biochemistry 33, 9762-9768.
• Unno, M., Christian, J.F., Benson, D.E., Gerber, N.C., Sligar, S.G. and Champion, P.M. (1997) Resonance Raman investigations of cytochrome P450_cam complexed with putidaredoxin. J. Am. Chem. Soc. 119, 6614-6620.
• Vidakovic, M., Sligar, S.G., Li, H. and Poulos, T.L. (1998) Understanding the role of the essential Asp251 in cytochrome P450cam using site-directed mutagenesis, crystallography, and kinetic solvent isotope effect. Biochemistry 37, 9211-9219.
• Wakasugi, K., Ishimori, K. and Morishima, I. (1996) NMR studies of recombinant cytochrome P450cam mutants. Biochimie 78, 763-770.
• Wells, A.V., Li, P., Champion, P.M., Martinis, S.A. and Sligar, S.G. (1992) Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420. Biochemistry 31, 4384-4393.
• Westlake, A.C.G., Harford-Cross, C.F., Donovan, J. and Wong, L.-L. (1999) Mutations of glutamate-84 at the putative potassium-binding site affect camphor binding and oxidation by cytochrome P450_cam. Eur. J. Biochem. 265, 929-935.
• Wilker, J.J., Dmochowski, I.J., Dawson, J.H., Winkler, J.R. and Gray, H.B. (1999) Substrates for rapid delivery of electrons and holes to buried active sites in proteins. Angew. Chem. Int. Ed. 38, 89-92.
• Wirtz, M., Klucik, J. and Rivera, M. (2000) Ferredoxin-mediated electrocatalytic dehalogenation of haloalkanes by cytochrome P450cam. J. Am. Chem. Soc. 122, 1047-1056.
• Yoshioka, S., Takahashi, S., Hori, H., Ishimori, K. and Morishima, I. (2001) Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450_cam. Eur. J. Biochem. 268, 252-259.
• Zhu, L., Sage, J.T. and Champion, P.M. (1993) Quantitative structural comparisons of heme protein crystals and solutions using resonance Raman spectroscopy. Biochemistry 32, 11181-11185.

Back to the Directory of P450-containing Systems home page:

Trieste site

Gödöllõ site