메뉴 건너뛰기




Volumn 50, Issue 6, 2011, Pages 1053-1069

Elucidating the role of the proximal cysteine hydrogen-bonding network in ferric cytochrome P450cam and corresponding mutants using magnetic circular dichroism spectroscopy

Author keywords

[No Author keywords available]

Indexed keywords

CHARGE TRANSFER TRANSITIONS; COORDINATION SPHERE; DFT CALCULATION; ELECTRONIC TRANSITION; FUNCTIONAL UNITS; HYDROGEN BONDING NETWORK; IN-PLANE; IRON CENTERS; LOW TEMPERATURES; LOWER ENERGIES; MAGNETIC CIRCULAR DICHROISM SPECTROSCOPY; NEGATIVE COMPONENTS; OSCILLATOR STRENGTHS; OUT-OF-PLANE; Q BANDS; SATURATION CURVE; SORET BANDS; SULFUR DONORS; THIOLATES; VARIABLE TEMPERATURE; WILD TYPES;

EID: 79851496468     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101911y     Document Type: Article
Times cited : (54)

References (98)
  • 2
    • 4644275807 scopus 로고    scopus 로고
    • Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes
    • Meunier, B., De Visser, S. P., and Shaik, S. (2004) Mechanism of oxidation reactions catalyzed by cytochrome P450 enzymes Chem. Rev. 104, 3947-3980
    • (2004) Chem. Rev. , vol.104 , pp. 3947
    • Meunier, B.1    De Visser, S.P.2    Shaik, S.3
  • 3
    • 33845281095 scopus 로고
    • Cytochrome P-450 and chloroperoxidase: Thiolate-ligated heme enzymes. Spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation
    • Dawson, J. H. and Sono, M. (1987) Cytochrome P-450 and chloroperoxidase: thiolate-ligated heme enzymes. Spectroscopic determination of their active-site structures and mechanistic implications of thiolate ligation Chem. Rev. 87, 1255-1276
    • (1987) Chem. Rev. , vol.87 , pp. 1255
    • Dawson, J.H.1    Sono, M.2
  • 6
    • 0026735580 scopus 로고
    • Nitric oxide synthase is a cytochrome P-450 type hemoprotein
    • White, K. A. and Marletta, M. A. (1992) Nitric oxide synthase is a cytochrome P-450 type hemoprotein Biochemistry 31, 6627-6631
    • (1992) Biochemistry , vol.31 , pp. 6627
    • White, K.A.1    Marletta, M.A.2
  • 7
    • 0030988217 scopus 로고    scopus 로고
    • Structure-function aspects in the nitric oxide synthases
    • Stuehr, D. J. (1997) Structure-function aspects in the nitric oxide synthases Annu. Rev. Pharmacol. Toxicol. 37, 339-359 (Pubitemid 27238880)
    • (1997) Annual Review of Pharmacology and Toxicology , vol.37 , pp. 339-359
    • Stuehr, D.J.1
  • 8
    • 0027975453 scopus 로고
    • Nitric oxide: A physiologic messenger molecule
    • Bredt, D. S. and Snyder, S. H. (1994) Nitric oxide: a physiologic messenger molecule Annu. Rev. Biochem. 63, 175-195
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 175
    • Bredt, D.S.1    Snyder, S.H.2
  • 10
    • 0023023246 scopus 로고
    • Physical methods in the study of the active site geometry of cytochromes P450
    • Lewis, D. F. V. (1986) Physical methods in the study of the active site geometry of cytochromes P450 Drug Metab. Rev. 17, 1
    • (1986) Drug Metab. Rev. , vol.17 , pp. 1
    • Lewis, D.F.V.1
  • 11
    • 0141611170 scopus 로고    scopus 로고
    • Prediction of drug metabolism: The case of cytochrome P450 2D6
    • Vermeulen, N. P. E. (2003) Prediction of drug metabolism: the case of cytochrome P450 2D6 Curr. Top. Med. Chem. 3, 1227-1239
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 1227-1239
    • Vermeulen, N.P.E.1
  • 12
    • 36849051197 scopus 로고    scopus 로고
    • 5 and their reductases - Promising targets for structural studies by advanced solid-state NMR spectroscopy
    • 5 and their reductases - promising targets for structural studies by advanced solid-state NMR spectroscopy Biochim. Biophys. Acta 1768, 3235-3259
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 3235
    • Durr, U.H.N.1    Waskell, L.2    Ayyalusamy, R.3
  • 13
    • 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 (Pubitemid 32565712)
    • (2001) Chemical Research in Toxicology , vol.14 , Issue.6 , pp. 611-650
    • Guengerich, F.P.1
  • 14
    • 0002148690 scopus 로고    scopus 로고
    • Active iron-oxo and iron-peroxo species in cytochromes P450 and peroxidases; Oxo-hydroxo tautomerism with water-soluble metalloporphyrins
    • Meunier, B. and Bernadou, J. (2000) Active iron-oxo and iron-peroxo species in cytochromes P450 and peroxidases; oxo-hydroxo tautomerism with water-soluble metalloporphyrins Struct. Bonding (Berlin) 97, 1-35
    • (2000) Struct. Bonding (Berlin) , vol.97 , pp. 1
    • Meunier, B.1    Bernadou, J.2
  • 15
    • 0035984571 scopus 로고    scopus 로고
    • Oxidizing species in the mechanism of cytochrome P450
    • Ortiz de Montellano, P. R. and De Voss, J. J. (2002) Oxidizing species in the mechanism of cytochrome P450 Nat. Prod. Rep. 19, 477-493
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 477
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 16
    • 0036197665 scopus 로고    scopus 로고
    • Theoretical study on kinetic isotope effects in the C-H bond activation of alkanes by iron-oxo complexes
    • Yoshizawa, K. (2002) Theoretical study on kinetic isotope effects in the C-H bond activation of alkanes by iron-oxo complexes Coord. Chem. Rev. 226, 251-259
    • (2002) Coord. Chem. Rev. , vol.226 , pp. 251-259
    • Yoshizawa, K.1
  • 17
    • 84962377244 scopus 로고    scopus 로고
    • A theoretical study on the mechanism of camphor hydroxylation by compound i of cytochrome P450
    • Kamachi, T. and Yoshizawa, K. (2003) A theoretical study on the mechanism of camphor hydroxylation by compound I of cytochrome P450 J. Am. Chem. Soc. 125, 4652-4661
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4652
    • Kamachi, T.1    Yoshizawa, K.2
  • 19
    • 0017302087 scopus 로고
    • Magnetic circular dichroism studies. 43. Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism
    • Dawson, J. H., Holm, R. H., Trudell, J. R., Barth, G., Linder, R. E., Bunnenberg, E., Djerassi, C., and Tang, S. C. (1976) Magnetic circular dichroism studies. 43. Oxidized cytochrome P-450. Magnetic circular dichroism evidence for thiolate ligation in the substrate-bound form. Implications for the catalytic mechanism J. Am. Chem. Soc. 98, 3707-3709
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 3707
    • Dawson, J.H.1    Holm, R.H.2    Trudell, J.R.3    Barth, G.4    Linder, R.E.5    Bunnenberg, E.6    Djerassi, C.7    Tang, S.C.8
  • 20
    • 0024294403 scopus 로고
    • Probing structure-function relations in heme-containing oxygenases and peroxidases
    • Dawson, J. H. (1988) Probing structure-function relations in heme-containing oxygenases and peroxidases Science 240, 433-439
    • (1988) Science , vol.240 , pp. 433-439
    • Dawson, J.H.1
  • 21
    • 69349100279 scopus 로고    scopus 로고
    • Characterization of the proximal ligand in P420 form of inducible nitric oxide synthase
    • Sabat, J., Stuehr, D. J., Yeh, S.-R., and Rousseau, D. L. (2009) Characterization of the proximal ligand in P420 form of inducible nitric oxide synthase J. Am. Chem. Soc. 131, 12186-12192
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 12186
    • Sabat, J.1    Stuehr, D.J.2    Yeh, S.-R.3    Rousseau, D.L.4
  • 22
    • 0034836145 scopus 로고    scopus 로고
    • Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam
    • Yoshioka, S., Takahashi, S., Hori, H., Ishimori, K., and Morishima, I. (2001) Proximal cysteine residue is essential for the enzymatic activities of cytochrome P450cam Eur. J. Biochem. 268, 252-259
    • (2001) Eur. J. Biochem. , vol.268 , pp. 252
    • Yoshioka, S.1    Takahashi, S.2    Hori, H.3    Ishimori, K.4    Morishima, I.5
  • 23
    • 0029800365 scopus 로고    scopus 로고
    • Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: Protein models for the active site of P450
    • Matsui, T. N., S., Ishimori, K., Watanabe, Y., and Morishima, I. (1996) Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: protein models for the active site of P450 Biochemistry 35, 13118-13124
    • (1996) Biochemistry , vol.35 , pp. 13118
    • Matsui, T.N.S.1    Ishimori, K.2    Watanabe, Y.3    Morishima, I.4
  • 24
    • 0030004641 scopus 로고    scopus 로고
    • Proton-assisted pathway to formation of the catalytically active, ferryl species of P450eryF
    • Harris, D. L. and Loew, G. H. (1996) Proton-assisted pathway to formation of the catalytically active, ferryl species of P450eryF J. Am. Chem. Soc. 118, 6377-6387
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 6377
    • Harris, D.L.1    Loew, G.H.2
  • 25
    • 0032500330 scopus 로고    scopus 로고
    • Theoretical investigation of the proton assisted pathway to formation of cytochrome P450 compound i
    • Harris, D. L. and Loew, G. H. (1998) Theoretical investigation of the proton assisted pathway to formation of cytochrome P450 compound I J. Am. Chem. Soc. 120, 8941-8948
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8941
    • Harris, D.L.1    Loew, G.H.2
  • 26
    • 0032556227 scopus 로고    scopus 로고
    • Role of the axial ligand in determining the spin state of resting cytochrome P450 [7]
    • DOI 10.1021/ja980994h
    • Green, M. T. (1998) Roles of the axial ligand in determining the spin state of resting cytochrome P450 J. Am. Chem. Soc. 120, 10772-10773 (Pubitemid 28498830)
    • (1998) Journal of the American Chemical Society , vol.120 , Issue.41 , pp. 10772-10773
    • Green, M.T.1
  • 27
    • 0033199376 scopus 로고    scopus 로고
    • Evidence for sulfur-based radicals in thiolate compound i intermediates
    • Green, M. T. (1999) Evidence for sulfur-based radicals in thiolate compound I intermediates J. Am. Chem. Soc. 121, 7939-7340
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 7939-7340
    • Green, M.T.1
  • 28
    • 0034823190 scopus 로고    scopus 로고
    • Multi-state epoxidation of ethene by cytochrome P450: A quantum chemical study
    • De Visser, S. P., Ogliaro, F., Harris, N., and Shaik, S. (2001) Multi-state epoxidation of ethene by cytochrome P450: a quantum chemical study J. Am. Chem. Soc. 123, 3037-3047
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3037
    • De Visser, S.P.1    Ogliaro, F.2    Harris, N.3    Shaik, S.4
  • 29
    • 58149173954 scopus 로고    scopus 로고
    • Multireference ab initio quantum mechanics/molecular mechanics study on intermediates in the catalytic cycle of cytochrome P450cam
    • Altun, A., Kumar, D., Neese, F., and Thiel, W. (2008) Multireference ab initio quantum mechanics/molecular mechanics study on intermediates in the catalytic cycle of cytochrome P450cam J. Phys. Chem. A 112, 12904-12910
    • (2008) J. Phys. Chem. A , vol.112 , pp. 12904
    • Altun, A.1    Kumar, D.2    Neese, F.3    Thiel, W.4
  • 30
    • 17744364713 scopus 로고    scopus 로고
    • Toward identification of the compound i reactive intermediate in cytochrome P450 chemistry: A QM/MM study of its EPR and MoÌ̂ssbauer parameters
    • Schoneboom, J. C., Neese, F., and Thiel, W. (2005) Toward identification of the compound I reactive intermediate in cytochrome P450 chemistry: a QM/MM study of its EPR and MoÌ̂ssbauer parameters J. Am. Chem. Soc. 127, 5840-5853
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 5840
    • Schoneboom, J.C.1    Neese, F.2    Thiel, W.3
  • 31
    • 0034692380 scopus 로고    scopus 로고
    • A model "rebound" mechanism of hydroxylation by cytochrome P450: Stepwise and effectively concerted pathways, and their reactivity patterns
    • Ogliaro, F., Harris, N., Cohen, S., Filatov, M., de Visser, S. P., and Shaik, S. (2000) A model "rebound" mechanism of hydroxylation by cytochrome P450: stepwise and effectively concerted pathways, and their reactivity patterns J. Am. Chem. Soc. 122, 8977-8989
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8977
    • Ogliaro, F.1    Harris, N.2    Cohen, S.3    Filatov, M.4    De Visser, S.P.5    Shaik, S.6
  • 32
    • 0142244914 scopus 로고    scopus 로고
    • How does product isotope effect prove the operation of a two-state "rebound" mechanism in C-H hydroxylation by cytochrome P450?
    • Kumar, D., de Visser, S. P., and Shaik, S. (2003) How does product isotope effect prove the operation of a two-state "rebound" mechanism in C-H hydroxylation by cytochrome P450? J. Am. Chem. Soc. 125, 13024-13025
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13024
    • Kumar, D.1    De Visser, S.P.2    Shaik, S.3
  • 33
    • 0033521186 scopus 로고    scopus 로고
    • On the "rebound" mechanism of alkane hydroxylation by cytochrome P450: Electronic structure of the intermediate and the electron transfer character in the rebound step
    • Filatov, M., Harris, N., and Shaik, S. (1999) On the "rebound" mechanism of alkane hydroxylation by cytochrome P450: Electronic structure of the intermediate and the electron transfer character in the rebound step Angew. Chem., Int. Ed. 38, 3510-3512
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 3510
    • Filatov, M.1    Harris, N.2    Shaik, S.3
  • 34
    • 0037014038 scopus 로고    scopus 로고
    • Hydrogen bonding modulates the selectivity of enzymatic oxidation by P450: Chameleon oxidant behavior by compound i
    • de Visser, S. P., Ogliaro, F., Sharma, P. K., and Shaik, S. (2002) Hydrogen bonding modulates the selectivity of enzymatic oxidation by P450: chameleon oxidant behavior by compound I Angew. Chem., Int. Ed. 41, 1947-1951
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 1947
    • De Visser, S.P.1    Ogliaro, F.2    Sharma, P.K.3    Shaik, S.4
  • 35
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T. L., Finzel, B. C., and Howard, A. J. (1987) High-resolution crystal structure of cytochrome P450cam J. Mol. Biol. 195, 687-700
    • (1987) J. Mol. Biol. , vol.195 , pp. 687
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 36
    • 0029586252 scopus 로고
    • Structure of cytochrome P450 eryF: An enzyme involved in erythromycin biosynthesis
    • Cupp-Vickery, J. and Poulos, T. L. (1995) Structure of cytochrome P450 eryF: an enzyme involved in erythromycin biosynthesis Nat. Struct. Biol. 2, 144-153
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 144
    • Cupp-Vickery, J.1    Poulos, T.L.2
  • 37
    • 0027326717 scopus 로고
    • Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450’s
    • Ravichandran, K. G., Boddupalli, S. S., Hasemann, C. A., Peterson, J., and Deisenhofer, J. (1993) Crystal structure of hemoprotein domain of P450BM-3, a prototype for microsomal P450’s Science 261, 731-736
    • (1993) Science , vol.261 , pp. 731
    • Ravichandran, K.G.1    Boddupalli, S.S.2    Hasemann, C.A.3    Peterson, J.4    Deisenhofer, J.5
  • 38
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • Hasemann, C. A., Ravichandran, K. G., Boddupalli, S. S., Peterson, J., and Deisenhofer, J. (1995) Structure and function of cytochromes P450: a comparative analysis of three crystal structures Structure 3, 41-62
    • (1995) Structure , vol.3 , pp. 41
    • Hasemann, C.A.1    Ravichandran, K.G.2    Boddupalli, S.S.3    Peterson, J.4    Deisenhofer, J.5
  • 39
    • 0037065303 scopus 로고    scopus 로고
    • Roles of the proximal hydrogen bonding network in cytochrome P450cam-catalyzed oxygenation
    • Yoshioka, S., Tosha, T., Takahashi, S., Ishimori, K., Hori, H., and Morishima, I. (2002) Roles of the proximal hydrogen bonding network in cytochrome P450cam-catalyzed oxygenation J. Am. Chem. Soc. 124, 14571-14579
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14571
    • Yoshioka, S.1    Tosha, T.2    Takahashi, S.3    Ishimori, K.4    Hori, H.5    Morishima, I.6
  • 40
    • 0001336179 scopus 로고    scopus 로고
    • Role of the invariant peptide fragment forming NH• •Â•S hydrogen bonds in the active site of cytochrome P-450 and chloroperoxidase: Synthesis and properties of Cys-containing peptide Fe(III) and Ga(III) (octaethylporphinato) complexes as models
    • Ueno, T., Nishikawa, N., Moriyama, S., Adachi, S., Lee, K., Okamura, T., Ueyama, N., and Nakamura, A. (1999) Role of the invariant peptide fragment forming NH•••S hydrogen bonds in the active site of cytochrome P-450 and chloroperoxidase: synthesis and properties of Cys-containing peptide Fe(III) and Ga(III) (octaethylporphinato) complexes as models Inorg. Chem. 38, 1199-1210
    • (1999) Inorg. Chem. , vol.38 , pp. 1199
    • Ueno, T.1    Nishikawa, N.2    Moriyama, S.3    Adachi, S.4    Lee, K.5    Okamura, T.6    Ueyama, N.7    Nakamura, A.8
  • 41
    • 0030455533 scopus 로고    scopus 로고
    • Cytochrome P-450 model (porphinato)(thiolato)iron(III) complexes with single and double NH•••S hydrogen bonds at the thiolate site
    • Ueyama, N., Nishikawa, N., Yamada, Y., Okamura, T., and Nakamura, A. (1996) Cytochrome P-450 model (porphinato)(thiolato)iron(III) complexes with single and double NH•••S hydrogen bonds at the thiolate site J. Am. Chem. Soc. 118, 12826-12827
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12826
    • Ueyama, N.1    Nishikawa, N.2    Yamada, Y.3    Okamura, T.4    Nakamura, A.5
  • 42
    • 0000653070 scopus 로고    scopus 로고
    • Synthesis and properties of octaethylporphinato(arenethiolato)iron(III) complexes with intramolecular NH•••S hydrogen bond: Chemical function of the hydrogen bond
    • Ueyama, N., Nishikawa, N., Yamada, Y., Okamura, T., Oka, S., Sakurai, H., and Nakamura, A. (1998) Synthesis and properties of octaethylporphinato(arenethiolato)iron(III) complexes with intramolecular NH•••S hydrogen bond: chemical function of the hydrogen bond Inorg. Chem. 37, 2415-2421
    • (1998) Inorg. Chem. , vol.37 , pp. 2415
    • Ueyama, N.1    Nishikawa, N.2    Yamada, Y.3    Okamura, T.4    Oka, S.5    Sakurai, H.6    Nakamura, A.7
  • 43
    • 0033572911 scopus 로고    scopus 로고
    • Novel iron porphyrin-alkanethiolate complex with intramolecular NH-S hydrogen bond: Synthesis, spectroscopy, and reactivity
    • Suzuki, N., Higuchi, T., Urano, Y., Kikuchi, K., Uekusa, H., Ohashi, Y., Uchida, T., Kitagawa, T., and Nigano, T. (1999) Novel iron porphyrin- alkanethiolate complex with intramolecular NH-S hydrogen bond: synthesis, spectroscopy, and reactivity J. Am. Chem. Soc. 121, 11571-11572
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 11571
    • Suzuki, N.1    Higuchi, T.2    Urano, Y.3    Kikuchi, K.4    Uekusa, H.5    Ohashi, Y.6    Uchida, T.7    Kitagawa, T.8    Nigano, T.9
  • 44
    • 67650549945 scopus 로고    scopus 로고
    • S K-edge XAS and DFT calculations on cytochrome P450: Covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity
    • Dey, A., Jiang, Y., Ortiz de Montellano, P. R., Hodgson, K. O., Hedman, B., and Solomon, E. I. (2009) S K-edge XAS and DFT calculations on cytochrome P450: covalent and ionic contributions to the cysteine-Fe bond and their contribution to reactivity J. Am. Chem. Soc. 131, 7869-7878
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 7869
    • Dey, A.1    Jiang, Y.2    Ortiz De Montellano, P.R.3    Hodgson, K.O.4    Hedman, B.5    Solomon, E.I.6
  • 45
    • 84961971288 scopus 로고    scopus 로고
    • Sulfur K-edge XAS and DFT calculations on P450 model complexes: Effects of hydrogen bonding on electronic structure and redox potentials
    • Dey, A., Okamura, T., Ueyama, N., Hedman, B., Hodgson, K. O., and Solomon, E. I. (2005) Sulfur K-edge XAS and DFT calculations on P450 model complexes: effects of hydrogen bonding on electronic structure and redox potentials J. Am. Chem. Soc. 127, 12046-12053
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 12046
    • Dey, A.1    Okamura, T.2    Ueyama, N.3    Hedman, B.4    Hodgson, K.O.5    Solomon, E.I.6
  • 46
    • 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
  • 47
    • 0024579824 scopus 로고
    • The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM
    • Raag, R. and Poulos, T. L. (1989) The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM Biochemistry 28, 917-922
    • (1989) Biochemistry , vol.28 , pp. 917
    • Raag, R.1    Poulos, T.L.2
  • 48
    • 0019890350 scopus 로고
    • Magnetic circular dichroism studies of cytochrome P450cam characterization of axial ligands of ferric and ferrous low-spin complexes
    • Shimizu, T., Iizuka, T., Shimada, H., Ishimura, Y., Nozawa, T., and Hatano, M. (1981) Magnetic circular dichroism studies of cytochrome P450cam characterization of axial ligands of ferric and ferrous low-spin complexes Biochim. Biophys. Acta 670, 341-354
    • (1981) Biochim. Biophys. Acta , vol.670 , pp. 341
    • Shimizu, T.1    Iizuka, T.2    Shimada, H.3    Ishimura, Y.4    Nozawa, T.5    Hatano, M.6
  • 49
    • 0020478791 scopus 로고
    • Spectroscopic investigations of ferric cytochrome P450cam ligand complexes
    • Dawson, J. H., Andersson, L. A., and Sono, M. (1982) Spectroscopic investigations of ferric cytochrome P450cam ligand complexes J. Biol. Chem. 257, 3606-3617
    • (1982) J. Biol. Chem. , vol.257 , pp. 3606
    • Dawson, J.H.1    Andersson, L.A.2    Sono, M.3
  • 51
    • 0019330820 scopus 로고
    • Electron paramagnetic resonance detectable states of cytochrome P-450cam
    • Lipscomb, J. D. (1980) Electron paramagnetic resonance detectable states of cytochrome P-450cam Biochemistry 19, 3590-3599
    • (1980) Biochemistry , vol.19 , pp. 3590-3599
    • Lipscomb, J.D.1
  • 52
    • 0028104429 scopus 로고
    • EPR studies on the photoproducts of ferric cytochrome P450cam (CYP101) nitrosyl complexes: Effects of camphor and its analogues on ligandbound structures
    • 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. 116, 1146-1152
    • (1994) J. Biochem. , vol.116 , pp. 1146
    • Masuya, F.1    Tsubaki, M.2    Makino, R.3    Hori, H.4
  • 55
    • 0001765497 scopus 로고
    • Magnetic circular dichroism
    • Stephens, P. J. (1974) Magnetic circular dichroism Annu. Rev. Phys. Chem. 25, 201-232
    • (1974) Annu. Rev. Phys. Chem. , vol.25 , pp. 201-232
    • Stephens, P.J.1
  • 56
    • 0001639366 scopus 로고
    • Magnetic circular dichroism
    • Stephens, P. J. (1976) Magnetic circular dichroism Adv. Chem. Phys. 35, 197-264
    • (1976) Adv. Chem. Phys. , vol.35 , pp. 197-264
    • Stephens, P.J.1
  • 57
    • 0029099527 scopus 로고
    • A ligand field model for MCD spectra of biological cupric complexes
    • Landrum, G. A., Ekberg, C. A., and Whittaker, J. W. (1995) A ligand field model for MCD spectra of biological cupric complexes Biophys. J. 69, 674-689
    • (1995) Biophys. J. , vol.69 , pp. 674
    • Landrum, G.A.1    Ekberg, C.A.2    Whittaker, J.W.3
  • 58
    • 0037397638 scopus 로고    scopus 로고
    • Recent applications of MCD spectroscopy to metalloenzymes
    • Kirk, M. L. and Peariso, K. (2003) Recent applications of MCD spectroscopy to metalloenzymes Curr. Opin. Chem. Biol. 7, 220-227
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 220
    • Kirk, M.L.1    Peariso, K.2
  • 61
    • 46749096032 scopus 로고    scopus 로고
    • Detailed assignment of the magnetic circular dichroism and UV-vis spectra of five-coordinate high-spin ferric [Fe(TPP)(Cl)]
    • Paulat, F. and Lehnert, N. (2008) Detailed assignment of the magnetic circular dichroism and UV-vis spectra of five-coordinate high-spin ferric [Fe(TPP)(Cl)] Inorg. Chem. 47, 4963-4976
    • (2008) Inorg. Chem. , vol.47 , pp. 4963
    • Paulat, F.1    Lehnert, N.2
  • 62
    • 33645890879 scopus 로고    scopus 로고
    • Quantum chemistry-based analysis of the vibrational spectra of five-coordinate metalloporphyrins [M(TPP)Cl]
    • Paulat, F., Praneeth, V. K. K., NaÌ̂ther, C., and Lehnert, N. (2006) Quantum chemistry-based analysis of the vibrational spectra of five-coordinate metalloporphyrins [M(TPP)Cl] Inorg. Chem. 45, 2835-2856
    • (2006) Inorg. Chem. , vol.45 , pp. 2835
    • Paulat, F.1    Praneeth, V.K.K.2    Naì̂ther, C.3    Lehnert, N.4
  • 63
    • 20144385036 scopus 로고    scopus 로고
    • Reaction of ferric cytochrome P450cam with peracids
    • Spolitak, T., Dawson, J. H., and Ballou, D. P. (2005) Reaction of ferric cytochrome P450cam with peracids J. Biol. Chem. 280, 20300-20309
    • (2005) J. Biol. Chem. , vol.280 , pp. 20300
    • Spolitak, T.1    Dawson, J.H.2    Ballou, D.P.3
  • 65
    • 0000189651 scopus 로고
    • Density-functional thermochemistry. III. The role of exact exchange
    • Becke, A. D. (1993) Density-functional thermochemistry. III. The role of exact exchange J. Chem. Phys. 98, 5648-5652
    • (1993) J. Chem. Phys. , vol.98 , pp. 5648-5652
    • Becke, A.D.1
  • 66
    • 0345491105 scopus 로고
    • Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density
    • Lee, C., Yang, W., and Parr, R. G. (1988) Development of the Colle-Salvetti correlation-energy formula into a functional of the electron density Phys. Rev. B (Condensed Matter) 37, 785-789
    • (1988) Phys. Rev. B (Condensed Matter) , vol.37 , pp. 785
    • Lee, C.1    Yang, W.2    Parr, R.G.3
  • 67
    • 33745770836 scopus 로고
    • Ab initio effective core potentials for molecular calculations. Potentials for the transition metal atoms Sc to Hg
    • Wadt, W. R. and Hay, P. J. (1985) Ab initio effective core potentials for molecular calculations. Potentials for the transition metal atoms Sc to Hg J. Chem. Phys. 82, 270-283
    • (1985) J. Chem. Phys. , vol.82 , pp. 270
    • Wadt, W.R.1    Hay, P.J.2
  • 68
    • 0006073669 scopus 로고
    • Ab initio effective core potentials for molecular calculations. Potentials for main group elements Na to Bi
    • Wadt, W. R. and Hay, P. J. (1985) Ab initio effective core potentials for molecular calculations. Potentials for main group elements Na to Bi J. Chem. Phys. 82, 284-298
    • (1985) J. Chem. Phys. , vol.82 , pp. 284
    • Wadt, W.R.1    Hay, P.J.2
  • 69
    • 27344448074 scopus 로고
    • Ab initio effective core potentials for molecular calculations. Potentials for K to Au including the outermost core orbitals
    • Wadt, W. R. and Hay, P. J. (1985) Ab initio effective core potentials for molecular calculations. Potentials for K to Au including the outermost core orbitals J. Chem. Phys. 82, 299-311
    • (1985) J. Chem. Phys. , vol.82 , pp. 299
    • Wadt, W.R.1    Hay, P.J.2
  • 71
    • 84961971217 scopus 로고    scopus 로고
    • Influence of molecular geometry, exchange-correlation functional, and solvent effects in the modeling of vertical excitation energies in phthalocyanines using time-dependent density functional theory (TDDFT) and polarized continuum model TDDFT methods: Can modern computational chemistry methods explain experimental controversies?
    • Nemykin, V. N., Hadt, R. G., Belosludov, R. N., Mizuseki, H., and Kawazoe, Y. (2007) Influence of molecular geometry, exchange-correlation functional, and solvent effects in the modeling of vertical excitation energies in phthalocyanines using time-dependent density functional theory (TDDFT) and polarized continuum model TDDFT methods: can modern computational chemistry methods explain experimental controversies? J. Phys. Chem. A 111, 12901-12913
    • (2007) J. Phys. Chem. A , vol.111 , pp. 12901
    • Nemykin, V.N.1    Hadt, R.G.2    Belosludov, R.N.3    Mizuseki, H.4    Kawazoe, Y.5
  • 72
    • 35848965262 scopus 로고    scopus 로고
    • Magnetic circular dichroism of porphyrins containing M = Ca, Ni, and Zn. A computational study based on time-dependent density functional theory
    • Peralta, G. A., Seth, M., and Ziegler, T. (2007) Magnetic circular dichroism of porphyrins containing M = Ca, Ni, and Zn. A computational study based on time-dependent density functional theory Inorg. Chem. 46, 9111-9125
    • (2007) Inorg. Chem. , vol.46 , pp. 9111
    • Peralta, G.A.1    Seth, M.2    Ziegler, T.3
  • 73
    • 69549135843 scopus 로고    scopus 로고
    • Sitting-atop metallo-porphyrin complexes: Experimental and theoretical investigations on such elusive species
    • De Luca, G., Romeo, A., Scolaro, L. M., Ricciardi, G., and A., R. (2009) Sitting-atop metallo-porphyrin complexes: experimental and theoretical investigations on such elusive species Inorg. Chem. 48, 8493-8507
    • (2009) Inorg. Chem. , vol.48 , pp. 8493
    • De Luca, G.1    Romeo, A.2    Scolaro, L.M.3    Ricciardi, G.4
  • 74
    • 4243553426 scopus 로고
    • Density-functional exchange-energy approximation with correct asymptotic behavior
    • Becke, A. D. (1988) Density-functional exchange-energy approximation with correct asymptotic behavior Phys. Rev. A 38, 3098-3100
    • (1988) Phys. Rev. A , vol.38 , pp. 3098-3100
    • Becke, A.D.1
  • 75
    • 5944261746 scopus 로고
    • Density-functional approximation for the correlation-energy of the inhomogeneous electron-gas
    • Perdew, J. P. (1986) Density-functional approximation for the correlation-energy of the inhomogeneous electron-gas Phys. Rev. B (Condensed Matter) 33, 8822-8824
    • (1986) Phys. Rev. B (Condensed Matter) , vol.33 , pp. 8822-8824
    • Perdew, J.P.1
  • 76
    • 26344435738 scopus 로고
    • Fully optimized contracted Gaussian basis sets for atoms Li to Kr
    • Schaefer, A., Horn, H., and Ahrichs, R. (1992) Fully optimized contracted Gaussian basis sets for atoms Li to Kr J. Chem. Phys. 97, 2571-2577
    • (1992) J. Chem. Phys. , vol.97 , pp. 2571
    • Schaefer, A.1    Horn, H.2    Ahrichs, R.3
  • 77
    • 0039209924 scopus 로고
    • Fully optimized contracted Gaussian basis sets of triple zeta valence quality for atoms Li to Kr
    • Schaefer, A., Huber, C., and Ahrichs, R. (1994) Fully optimized contracted Gaussian basis sets of triple zeta valence quality for atoms Li to Kr J. Chem. Phys. 100, 5829-5835
    • (1994) J. Chem. Phys. , vol.100 , pp. 5829
    • Schaefer, A.1    Huber, C.2    Ahrichs, R.3
  • 78
    • 70549104970 scopus 로고    scopus 로고
    • ORCA 2.4 ed., UniversitaÌ̂t Bonn, Bonn, Germany
    • Neese, F. (2004) ORCA, ORCA 2.4 ed., UniversitaÌ̂t Bonn, Bonn, Germany.
    • (2004) ORCA
    • Neese, F.1
  • 79
    • 0001479052 scopus 로고    scopus 로고
    • MCD C-term signs, saturation behavior, and determination of band polarizations in randomly oriented systems with spin S ≥ 1/2. Applications to S = 1/2 and S = 5/2
    • Neese, F. and Solomon, E. I. (1999) MCD C-term signs, saturation behavior, and determination of band polarizations in randomly oriented systems with spin S ≥ 1/2. Applications to S = 1/2 and S = 5/2 Inorg. Chem. 38, 1847-1865
    • (1999) Inorg. Chem. , vol.38 , pp. 1847
    • Neese, F.1    Solomon, E.I.2
  • 80
    • 79851490321 scopus 로고    scopus 로고
    • Personal communication
    • Spolitak, T. and Ballou, D. P. (2008) Personal communication.
    • (2008)
    • Spolitak, T.1    Ballou, D.P.2
  • 82
    • 0042813364 scopus 로고
    • Spectra of porphyrins
    • Gouterman, M. (1961) Spectra of porphyrins J. Mol. Spectrosc. 6, 138-163
    • (1961) J. Mol. Spectrosc. , vol.6 , pp. 138-163
    • Gouterman, M.1
  • 83
    • 0347021893 scopus 로고
    • Study of the effects of substitution on the absorption spectra of porphyrin
    • Gouterman, M. (1959) Study of the effects of substitution on the absorption spectra of porphyrin J. Chem. Phys. 30, 1139-1161
    • (1959) J. Chem. Phys. , vol.30 , pp. 1139-1161
    • Gouterman, M.1
  • 85
    • 0342674893 scopus 로고    scopus 로고
    • Computational modeling of metalloporphyrin structure and vibrational spectra: Porphyrin ruffling in NiTPP
    • Rush, T. S., III, Kozlowski, P. M., Piffat, C. A., Kumble, R., Zgierski, M. Z., and Spiro, T. G. (2000) Computational modeling of metalloporphyrin structure and vibrational spectra: porphyrin ruffling in NiTPP J. Phys. Chem. B 104, 5020-5034
    • (2000) J. Phys. Chem. B , vol.104 , pp. 5020
    • Rush III, T.S.1    Kozlowski, P.M.2    Piffat, C.A.3    Kumble, R.4    Zgierski, M.Z.5    Spiro, T.G.6
  • 86
    • 33645870443 scopus 로고    scopus 로고
    • Spectroscopic properties and electronic structure of five- and six-coordinate iron(II) porphyrin NO complexes: Effect of the axial N-donor ligand
    • Praneeth, V. K. K., NaÌ̂ther, C., Peters, G., and Lehnert, N. (2006) Spectroscopic properties and electronic structure of five- and six-coordinate iron(II) porphyrin NO complexes: effect of the axial N-donor ligand Inorg. Chem. 45, 2795-2811
    • (2006) Inorg. Chem. , vol.45 , pp. 2795
    • Praneeth, V.K.K.1    Naì̂ther, C.2    Peters, G.3    Lehnert, N.4
  • 87
    • 84882882718 scopus 로고    scopus 로고
    • Electron paramagnetic resonance and low-temperature magnetic circular dichroism spectroscopy of ferrous heme nitrosyls
    • Elsevier, Amsterdam
    • Lehnert, N. (2008) Electron paramagnetic resonance and low-temperature magnetic circular dichroism spectroscopy of ferrous heme nitrosyls, in The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins (Ghosh, A., Ed.) pp 147 - 171, Elsevier, Amsterdam.
    • (2008) The Smallest Biomolecules: Diatomics and Their Interactions with Heme Proteins , pp. 147-171
    • Lehnert, N.1    Ghosh, A.2
  • 90
    • 0001417351 scopus 로고
    • Investigations of the resonance Raman excitation profiles of cytochrome P450cam
    • Bangcharoenpaurpong, O., Champion, P. M., Martinis, S. A., and Sligar, S. G. (1987) Investigations of the resonance Raman excitation profiles of cytochrome P450cam J. Chem. Phys. 87, 4273-4284
    • (1987) J. Chem. Phys. , vol.87 , pp. 4273
    • Bangcharoenpaurpong, O.1    Champion, P.M.2    Martinis, S.A.3    Sligar, S.G.4
  • 92
    • 0037389596 scopus 로고    scopus 로고
    • Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: Stability, structure, and dynamics of axial ligand complexes
    • Shokhireva, T. K., Berry, R. E., Uno, E., Balfour, C. A., Zhang, H., and Walker, F. A. (2003) Electrochemical and NMR spectroscopic studies of distal pocket mutants of nitrophorin 2: stability, structure, and dynamics of axial ligand complexes Proc. Natl. Acad. Sci. U.S.A. 100, 3778-3783
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3778
    • Shokhireva, T.K.1    Berry, R.E.2    Uno, E.3    Balfour, C.A.4    Zhang, H.5    Walker, F.A.6
  • 93
    • 33947358104 scopus 로고    scopus 로고
    • Electronic structure of ferric heme nitrosyl complexes with thiolate coordination
    • Paulat, F. and Lehnert, N. (2007) Electronic structure of ferric heme nitrosyl complexes with thiolate coordination Inorg. Chem. 46, 1547-1549
    • (2007) Inorg. Chem. , vol.46 , pp. 1547
    • Paulat, F.1    Lehnert, N.2
  • 94
    • 0019082049 scopus 로고
    • Magnetization curves of haemoproteins measured by low-temperature magnetic-circular-dichroism spectroscopy
    • Thomson, A. J. and Johnson, A. K. (1980) Magnetization curves of haemoproteins measured by low-temperature magnetic-circular-dichroism spectroscopy Biochem. J. 191, 411-420
    • (1980) Biochem. J. , vol.191 , pp. 411
    • Thomson, A.J.1    Johnson, A.K.2
  • 96
    • 5644282610 scopus 로고    scopus 로고
    • Crystal structure of the cytochrome P450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding
    • Nagano, S., Tosha, T., Ishimori, K., Morishima, I., and Poulos, T. L. (2004) Crystal structure of the cytochrome P450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding J. Biochem. Chem. 279, 42844-42849
    • (2004) J. Biochem. Chem. , vol.279 , pp. 42844
    • Nagano, S.1    Tosha, T.2    Ishimori, K.3    Morishima, I.4    Poulos, T.L.5
  • 98
    • 0001851317 scopus 로고    scopus 로고
    • The role of the proximal ligand in heme enzymes
    • Poulos, T. L. (1996) The role of the proximal ligand in heme enzymes J. Biol. Inorg. Chem. 1, 356-359 (Pubitemid 126490024)
    • (1996) Journal of Biological Inorganic Chemistry , vol.1 , Issue.4 , pp. 356-359
    • Poulos, T.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.