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Volumn 53, Issue 9, 2014, Pages 1428-1434

Strength of axial water ligation in substrate-free cytochrome P450s is isoform dependent

Author keywords

[No Author keywords available]

Indexed keywords

AXIAL LIGAND; HIGH SPIN STATE; LIGAND FIELD; MAGNETIC CIRCULAR DICHROISMS; NEAR-INFRARED BANDS; RESTING STATE; SPIN STATE; SUBSTRATE-FREE;

EID: 84896072869     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi401547j     Document Type: Article
Times cited : (21)

References (37)
  • 2
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • Guengerich, F. P. (2001) Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity Chem. Res. Toxicol. 14, 611-650
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 3
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibriums in cytochrome P450
    • Sligar, S. G. (1976) Coupling of spin, substrate, and redox equilibriums in cytochrome P450 Biochemistry 15, 5399-5406
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 4
    • 33845379583 scopus 로고
    • Control of heme protein redox potential and reduction rate: Linear free energy relation between potential and ferric spin state equilibrium
    • Fisher, M. T. and Sligar, S. G. (1985) Control of heme protein redox potential and reduction rate: linear free energy relation between potential and ferric spin state equilibrium J. Am. Chem. Soc. 107, 5018-5019
    • (1985) J. Am. Chem. Soc. , vol.107 , pp. 5018-5019
    • Fisher, M.T.1    Sligar, S.G.2
  • 5
    • 13444287729 scopus 로고    scopus 로고
    • The thermodynamic landscape of testosterone binding to cytochrome P450 3A4: Ligand binding and spin state equilibria
    • Roberts, A. G., Campbell, A. P., and Atkins, W. M. (2005) The thermodynamic landscape of testosterone binding to cytochrome P450 3A4: ligand binding and spin state equilibria Biochemistry 44, 1353-1366
    • (2005) Biochemistry , vol.44 , pp. 1353-1366
    • Roberts, A.G.1    Campbell, A.P.2    Atkins, W.M.3
  • 7
    • 0029942501 scopus 로고    scopus 로고
    • Study of water binding to low spin Fe(III) in cytochrome P450 by pulsed ENDOR and four-pulse ESEEM spectroscopies
    • Goldfarb, D., Bernardo, M., Thomann, H., Kroneck, P. M. H., and Ullrich, V. (1996) Study of water binding to low spin Fe(III) in cytochrome P450 by pulsed ENDOR and four-pulse ESEEM spectroscopies J. Am. Chem. Soc. 118, 2686-2693
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2686-2693
    • Goldfarb, D.1    Bernardo, M.2    Thomann, H.3    Kroneck, P.M.H.4    Ullrich, V.5
  • 9
    • 34547696989 scopus 로고    scopus 로고
    • Control by substrate of the cytochrome P450-dependent redox machinery: Mechanistic insights
    • Hlavica, P. (2007) Control by substrate of the cytochrome P450-dependent redox machinery: mechanistic insights Curr. Drug Metab. 8, 594-611
    • (2007) Curr. Drug Metab. , vol.8 , pp. 594-611
    • Hlavica, P.1
  • 10
    • 84872840358 scopus 로고    scopus 로고
    • Oxidase uncoupling in heme monooxygenases: Human cytochrome P450 CYP3A4 in Nanodiscs
    • Grinkova, Y. V., Denisov, I. G., McLean, M. A., and Sligar, S. G. (2013) Oxidase uncoupling in heme monooxygenases: Human cytochrome P450 CYP3A4 in Nanodiscs Biochem. Biophys. Res. Commun. 430, 1223-1227
    • (2013) Biochem. Biophys. Res. Commun. , vol.430 , pp. 1223-1227
    • Grinkova, Y.V.1    Denisov, I.G.2    McLean, M.A.3    Sligar, S.G.4
  • 11
    • 0028023169 scopus 로고
    • Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties
    • Gillam, E. M. J., Guo, Z. Y., and Guengerich, F. P. (1994) Expression of modified human cytochrome P450 2E1 in Escherichia coli, purification, and spectral and catalytic properties Arch. Biochem. Biophys. 312, 59-66
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 59-66
    • Gillam, E.M.J.1    Guo, Z.Y.2    Guengerich, F.P.3
  • 13
    • 84856477784 scopus 로고    scopus 로고
    • Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001
    • DeVore, N. M. and Scott, E. E. (2012) Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001 Nature 482, 116-119
    • (2012) Nature , vol.482 , pp. 116-119
    • Devore, N.M.1    Scott, E.E.2
  • 14
    • 80052944899 scopus 로고    scopus 로고
    • Direct spectroscopic evidence for binding of anastrozole to the iron heme of human aromatase. Peering into the mechanism of aromatase inhibition
    • Maurelli, S., Chiesa, M., Giamello, E., Di Nardo, G., V. Ferrero, V. E., Gilardi, G., and Van Doorslaer, S. (2011) Direct spectroscopic evidence for binding of anastrozole to the iron heme of human aromatase. Peering into the mechanism of aromatase inhibition Chem. Commun. 47, 10737-10739
    • (2011) Chem. Commun. , vol.47 , pp. 10737-10739
    • Maurelli, S.1    Chiesa, M.2    Giamello, E.3    Di Nardo, G.4    Ferrero, V.E.V.5    Gilardi, G.6    Van Doorslaer, S.7
  • 15
    • 81255195359 scopus 로고    scopus 로고
    • Allosteric activation of cytochrome P450 3A4 by alpha-naphthoflavone: Branch point regulation revealed by isotope dilution analysis
    • Woods, C. M., Fernandez, C., Kunze, K. L., and Atkins, W. M. (2012) Allosteric activation of cytochrome P450 3A4 by alpha-naphthoflavone: branch point regulation revealed by isotope dilution analysis Biochemistry 50, 10041-10051
    • (2012) Biochemistry , vol.50 , pp. 10041-10051
    • Woods, C.M.1    Fernandez, C.2    Kunze, K.L.3    Atkins, W.M.4
  • 17
    • 33745832316 scopus 로고    scopus 로고
    • Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions
    • McLean, K. J., Warman, A. J., Seward, H. E., Marshall, K. R., Girvan, H. M., Cheesman, M. R., Waterman, M. R., and Munro, A. W. (2006) Biophysical characterization of the sterol demethylase P450 from Mycobacterium tuberculosis, its cognate ferredoxin, and their interactions Biochemistry 45, 8427-8443
    • (2006) Biochemistry , vol.45 , pp. 8427-8443
    • McLean, K.J.1    Warman, A.J.2    Seward, H.E.3    Marshall, K.R.4    Girvan, H.M.5    Cheesman, M.R.6    Waterman, M.R.7    Munro, A.W.8
  • 18
    • 61449218869 scopus 로고    scopus 로고
    • Reaction of Mycobacterium tuberculosis cytochrome P450 enzymes with nitric oxide
    • Ouellet, H., Lang, J. r. m., Couture, M., and Ortiz de Montellano, P. R. (2009) Reaction of Mycobacterium tuberculosis cytochrome P450 enzymes with nitric oxide Biochemistry 48, 863-872
    • (2009) Biochemistry , vol.48 , pp. 863-872
    • Ouellet, H.1    Lang, J.R.M.2    Couture, M.3    Ortiz De Montellano, P.R.4
  • 19
    • 78651165715 scopus 로고
    • The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature
    • Omura, T. and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes: I. Evidence for its hemoprotein nature J. Biol. Chem. 239, 2370-2378
    • (1964) J. Biol. Chem. , vol.239 , pp. 2370-2378
    • Omura, T.1    Sato, R.2
  • 21
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll, S. and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR J. Magn. Reson. 178, 42-55
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 22
    • 0017593566 scopus 로고
    • The EPR of low spin heme complexes relation of the t2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters
    • Taylor, C. P. S. (1977) The EPR of low spin heme complexes relation of the t2g hole model to the directional properties of the g tensor, and a new method for calculating the ligand field parameters Biochim. Biophys. Acta-Protein Struct. 491, 137-148
    • (1977) Biochim. Biophys. Acta - Protein Struct. , vol.491 , pp. 137-148
    • Taylor, C.P.S.1
  • 23
    • 0029982945 scopus 로고    scopus 로고
    • Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes
    • Renaud, J. P. (1996) Thermodynamic studies of substrate binding and spin transitions in human cytochrome P-450 3A4 expressed in yeast microsomes Biochem. J. 319, 675-681
    • (1996) Biochem. J. , vol.319 , pp. 675-681
    • Renaud, J.P.1
  • 24
    • 83455163134 scopus 로고    scopus 로고
    • The structural basis for homotropic and heterotropic cooperativity of midazolam metabolism by human cytochrome P450 3A4
    • Roberts, A. G., Yang, J., Halpert, J. R., Nelson, S. D., Thummel, K. T., and Atkins, W. M. (2011) The structural basis for homotropic and heterotropic cooperativity of midazolam metabolism by human cytochrome P450 3A4 Biochemistry 50, 10804-10818
    • (2011) Biochemistry , vol.50 , pp. 10804-10818
    • Roberts, A.G.1    Yang, J.2    Halpert, J.R.3    Nelson, S.D.4    Thummel, K.T.5    Atkins, W.M.6
  • 26
    • 33846612045 scopus 로고
    • Infrared magnetic circular dichroism in the study of metalloproteins
    • Cheng, J. C., Osborne, G. A., Stephens, P. J., and Eaton, W. A. (1973) Infrared magnetic circular dichroism in the study of metalloproteins Nature 241, 193-194
    • (1973) Nature , vol.241 , pp. 193-194
    • Cheng, J.C.1    Osborne, G.A.2    Stephens, P.J.3    Eaton, W.A.4
  • 27
    • 0033464509 scopus 로고    scopus 로고
    • Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low spin ferriheme centers and their corresponding heme proteins
    • Walker, F. A. (1999) Magnetic spectroscopic (EPR, ESEEM, Mössbauer, MCD and NMR) studies of low spin ferriheme centers and their corresponding heme proteins Coord. Chem. Rev. 185-186, 471-534
    • (1999) Coord. Chem. Rev. , vol.185-186 , pp. 471-534
    • Walker, F.A.1
  • 28
    • 0027298183 scopus 로고
    • Identification of charge-transfer transitions in the optical spectrum of low spin ferric cytochrome P-450 Bacillus megaterium
    • McKnight, J., Cheesman, M. R., Thomson, A. J., Miles, J. S., and Munro, A. W. (1993) Identification of charge-transfer transitions in the optical spectrum of low spin ferric cytochrome P-450 Bacillus megaterium Eur. J. Biochem. 213, 683-687
    • (1993) Eur. J. Biochem. , vol.213 , pp. 683-687
    • McKnight, J.1    Cheesman, M.R.2    Thomson, A.J.3    Miles, J.S.4    Munro, A.W.5
  • 29
    • 37049070226 scopus 로고
    • A theoretical model of the intensity of the near-infrared porphyrin-to-iron charge-transfer transitions in low spin iron(III) haemoproteins. A correlation between the intensity of the magnetic circular dichroism bands and the rhombic distortion parameter of iron
    • Thomson, A. J. and Gadsby, P. M. A. (1990) A theoretical model of the intensity of the near-infrared porphyrin-to-iron charge-transfer transitions in low spin iron(III) haemoproteins. A correlation between the intensity of the magnetic circular dichroism bands and the rhombic distortion parameter of iron J. Chem. Soc., Dalton Trans. 0, 1921-1928
    • (1990) J. Chem. Soc., Dalton Trans. , vol.0 , pp. 1921-1928
    • Thomson, A.J.1    Gadsby, P.M.A.2
  • 30
    • 33751021526 scopus 로고
    • Binding in haemolglobin azide as determined by electron resonance: Theory of electron resonance in ferrihaemoglobin azide
    • Griffith, J. S. (1957) Binding in haemolglobin azide as determined by electron resonance: theory of electron resonance in ferrihaemoglobin azide Nature 180, 30-31
    • (1957) Nature , vol.180 , pp. 30-31
    • Griffith, J.S.1
  • 31
    • 0015560453 scopus 로고
    • Optical and magnetic probes of the structure of cytochrome P-450s
    • Peisach, J., Stern, J. O., and Blumberg, W. E. (1973) Optical and magnetic probes of the structure of cytochrome P-450s Drug Metab. Dispos. 1, 45-61
    • (1973) Drug Metab. Dispos. , vol.1 , pp. 45-61
    • Peisach, J.1    Stern, J.O.2    Blumberg, W.E.3
  • 32
    • 72149102431 scopus 로고    scopus 로고
    • The structure of Mycobacterium tuberculosis CYP125: Molecular basis for cholesterol binding in a P450 needed for host infection
    • McLean, K. J., Lafite, P., Levy, C., Cheesman, M. R., Mast, N., Pikuleva, I. A., Leys, D., and Munro, A. W. (2009) The structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection J. Biol. Chem. 284, 35524-35533
    • (2009) J. Biol. Chem. , vol.284 , pp. 35524-35533
    • McLean, K.J.1    Lafite, P.2    Levy, C.3    Cheesman, M.R.4    Mast, N.5    Pikuleva, I.A.6    Leys, D.7    Munro, A.W.8
  • 33
    • 0001731004 scopus 로고
    • Assignment of the axial ligands of ferric ion in low spin hemoproteins by near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy
    • Gadsby, P. M. A. and Thomson, A. J. (1990) Assignment of the axial ligands of ferric ion in low spin hemoproteins by near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy J. Am. Chem. Soc. 112, 5003-5011
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5003-5011
    • Gadsby, P.M.A.1    Thomson, A.J.2
  • 34
    • 33846958772 scopus 로고    scopus 로고
    • Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets: New heme ligation states influence conformational equilibria in P450 BM3
    • Girvan, H. M., Seward, H. E., Toogood, H. S., Cheesman, M. R., Leys, D., and Munro, A. W. (2007) Structural and spectroscopic characterization of P450 BM3 mutants with unprecedented P450 heme iron ligand sets: new heme ligation states influence conformational equilibria in P450 BM3 J. Biol. Chem. 282, 564-572
    • (2007) J. Biol. Chem. , vol.282 , pp. 564-572
    • Girvan, H.M.1    Seward, H.E.2    Toogood, H.S.3    Cheesman, M.R.4    Leys, D.5    Munro, A.W.6
  • 36
    • 0037028549 scopus 로고    scopus 로고
    • Spectroscopic studies of Pyrococcus furiosus superoxide reductase: Implications for active-site structures and the catalytic mechanism
    • Clay, M. D., Jenney, F. E., Hagedoorn, P. L., George, G. N., Adams, M. W. W., and Johnson, M. K. (2001) Spectroscopic studies of Pyrococcus furiosus superoxide reductase: implications for active-site structures and the catalytic mechanism J. Am. Chem. Soc. 124, 788-805
    • (2001) J. Am. Chem. Soc. , vol.124 , pp. 788-805
    • Clay, M.D.1    Jenney, F.E.2    Hagedoorn, P.L.3    George, G.N.4    Adams, M.W.W.5    Johnson, M.K.6
  • 37
    • 84861097117 scopus 로고    scopus 로고
    • Elucidating second coordination sphere effects in heme proteins using low-temperature magnetic circular dichroism spectroscopy
    • Lehnert, N. (2012) Elucidating second coordination sphere effects in heme proteins using low-temperature magnetic circular dichroism spectroscopy J. Inorg. Biochem. 110, 83-93
    • (2012) J. Inorg. Biochem. , vol.110 , pp. 83-93
    • Lehnert, N.1


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