메뉴 건너뛰기




Volumn 47, Issue 12, 2008, Pages 3950-3963

Resonance Raman studies of cytochrome P450 2B4 in its interactions with substrates and redox partners

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALS; MOLECULAR DYNAMICS; MOLECULAR INTERACTIONS; MOLECULAR STRUCTURE; REDOX REACTIONS; SUBSTRATES;

EID: 41149157449     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi800034b     Document Type: Article
Times cited : (21)

References (63)
  • 1
    • 13844322067 scopus 로고    scopus 로고
    • Cytochrome P450: Nature's Most Versatile Biological Catalyst
    • Coon, M. J. (2005) Cytochrome P450: Nature's Most Versatile Biological Catalyst. Annu. Rev. Pharmacol. Toxicol. 45, 1-25.
    • (2005) Annu. Rev. Pharmacol. Toxicol , vol.45 , pp. 1-25
    • Coon, M.J.1
  • 2
    • 36048939609 scopus 로고    scopus 로고
    • Mechanisms of cytochrome P450 substrate oxidation
    • Guengerich, P. F. (2007) Mechanisms of cytochrome P450 substrate oxidation. J. Biochem. Toxicol. 21, 163-168.
    • (2007) J. Biochem. Toxicol , vol.21 , pp. 163-168
    • Guengerich, P.F.1
  • 4
    • 33846373967 scopus 로고    scopus 로고
    • Structure-function analysis of cytochromes P450 2B
    • Zhao, Y., and Halpert, J. R. (2007) Structure-function analysis of cytochromes P450 2B. Biochim. Biophys. Acta 1770, 402-412.
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 402-412
    • Zhao, Y.1    Halpert, J.R.2
  • 5
    • 35648963202 scopus 로고    scopus 로고
    • 5 increases the rate of product formation by cytochrome P450 2B4 and competes with cytochrome P450 reductase for a binding site on cytochrome P450 2B4
    • 5 increases the rate of product formation by cytochrome P450 2B4 and competes with cytochrome P450 reductase for a binding site on cytochrome P450 2B4. J. Biol. Chem. 282, 29766-29776.
    • (2007) J. Biol. Chem , vol.282 , pp. 29766-29776
    • Zhang, H.1    Im, S.-C.2    Waskell, L.3
  • 6
    • 4644317084 scopus 로고    scopus 로고
    • Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions
    • Shengxi, J., Bryson, T. A., and Dawson, J. H. (2004) Hydroperoxoferric heme intermediate as a second electrophilic oxidant in cytochrome P450-catalyzed reactions. J. Biol. Inorg. Chem. 9, 644-653.
    • (2004) J. Biol. Inorg. Chem , vol.9 , pp. 644-653
    • Shengxi, J.1    Bryson, T.A.2    Dawson, J.H.3
  • 9
    • 0000740326 scopus 로고    scopus 로고
    • Resonance Raman spectra of heme proteins and model compounds
    • Kadish, K. M, Smith, K. M, and Guilard, R, Eds, Academic Press, New York
    • Kincaid, J. R. (2000) Resonance Raman spectra of heme proteins and model compounds, in Porphyrin Handbook (Kadish, K. M., Smith, K. M., and Guilard, R., Eds.) Vol. 7, pp 225-291, Academic Press, New York.
    • (2000) Porphyrin Handbook , vol.7 , pp. 225-291
    • Kincaid, J.R.1
  • 10
    • 0028223077 scopus 로고
    • How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models
    • Ray, G. B., Li, X. Y., Ibers, J. A., Sessler, J. L., and Spiro, T. G. (1994) How far can proteins bend the FeCO unit? Distal polar and steric effects in heme proteins and models. J. Am. Chem. Soc. 116, 162-176.
    • (1994) J. Am. Chem. Soc , vol.116 , pp. 162-176
    • Ray, G.B.1    Li, X.Y.2    Ibers, J.A.3    Sessler, J.L.4    Spiro, T.G.5
  • 11
    • 0027096191 scopus 로고
    • Hydrogen bonding of iron-coordinated histidine in heme proteins
    • Rousseau, D. G., and Rousseau, D. L. (1992) Hydrogen bonding of iron-coordinated histidine in heme proteins. J. Struct. Biol. 109, 13-17.
    • (1992) J. Struct. Biol , vol.109 , pp. 13-17
    • Rousseau, D.G.1    Rousseau, D.L.2
  • 12
    • 0017047120 scopus 로고
    • An anomaly in the resonance Raman spectra of cytochrome P-450cam in the ferrous high-spin state
    • Ozaki, Y., Kitagawa, T., Kyogoku, Y., Shimada, H., Iizuka, T., and Ishimura, Y. (1976) An anomaly in the resonance Raman spectra of cytochrome P-450cam in the ferrous high-spin state. J. Biochem. (Tokyo) 80, 1447-1451.
    • (1976) J. Biochem. (Tokyo) , vol.80 , pp. 1447-1451
    • Ozaki, Y.1    Kitagawa, T.2    Kyogoku, Y.3    Shimada, H.4    Iizuka, T.5    Ishimura, Y.6
  • 13
    • 33947094617 scopus 로고
    • Resonance Raman investigations of cytochrome P450cam from Pseudomonas putida
    • Champion, P. M., Gunsalus, I. C., and Wagner, G. C. (1978) Resonance Raman investigations of cytochrome P450cam from Pseudomonas putida. J. Am. Chem. Soc. 100, 3743-3751.
    • (1978) J. Am. Chem. Soc , vol.100 , pp. 3743-3751
    • Champion, P.M.1    Gunsalus, I.C.2    Wagner, G.C.3
  • 14
    • 0001474579 scopus 로고
    • Resonance Raman detection of an iron-sulfur bond in cytochrome P 450cam
    • Champion, P. M., Stallard, B. R., Wagner, G. C., and Gunsalus, I. C. (1982) Resonance Raman detection of an iron-sulfur bond in cytochrome P 450cam. J. Am. Chem. Soc. 104, 5469-5472.
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 5469-5472
    • Champion, P.M.1    Stallard, B.R.2    Wagner, G.C.3    Gunsalus, I.C.4
  • 15
    • 0021958596 scopus 로고
    • The resonance Raman frequencies of the iron-carbon monoxide stretching and bending modes in the carbon monoxide complex of cytochrome P-450cam
    • Uno, T., Nishimura, Y., Makino, R., Iizuka, T., Ishimura, Y., and Tsuboi, M. (1985) The resonance Raman frequencies of the iron-carbon monoxide stretching and bending modes in the carbon monoxide complex of cytochrome P-450cam. J. Biol. Chem. 260, 2023-2026.
    • (1985) J. Biol. Chem , vol.260 , pp. 2023-2026
    • Uno, T.1    Nishimura, Y.2    Makino, R.3    Iizuka, T.4    Ishimura, Y.5    Tsuboi, M.6
  • 16
    • 0026683129 scopus 로고
    • Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420
    • 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.
    • (1992) Biochemistry , vol.31 , pp. 4384-4393
    • Wells, A.V.1    Li, P.2    Champion, P.M.3    Martinis, S.A.4    Sligar, S.G.5
  • 17
    • 0033585577 scopus 로고    scopus 로고
    • Identification of the Fe-O-O Bending Mode in Oxycytochrome P450cam by Resonance Raman Spectroscopy
    • 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.
    • (1999) J. Am. Chem. Soc , vol.121 , pp. 376-380
    • Macdonald, I.D.G.1    Sligar, S.G.2    Christian, J.F.3    Unno, M.4    Champion, P.M.5
  • 18
    • 1242330313 scopus 로고    scopus 로고
    • Phe393 Mutants of Cytochrome P450 BM3 with Modified Heme Redox Potentials Have Altered Heme Vinyl and Propionate Conformations
    • Chen, Z., Ost, T. W. B., and Schelvis, J. P. M. (2004) Phe393 Mutants of Cytochrome P450 BM3 with Modified Heme Redox Potentials Have Altered Heme Vinyl and Propionate Conformations. Biochemistry 43, 1798-1808.
    • (2004) Biochemistry , vol.43 , pp. 1798-1808
    • Chen, Z.1    Ost, T.W.B.2    Schelvis, J.P.M.3
  • 19
    • 0035900956 scopus 로고    scopus 로고
    • Hydrogen-Bonding Interactions in the Active Sites of Cytochrome P450cam and Its Site-Directed Mutants
    • Deng, T.-J., Macdonald, I. D. G., Simianu, M. C., Sykora, M., Kincaid, J. R., and Sligar, S. G. (2001) Hydrogen-Bonding Interactions in the Active Sites of Cytochrome P450cam and Its Site-Directed Mutants. J. Am. Chem. Soc. 123, 269-278.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 269-278
    • Deng, T.-J.1    Macdonald, I.D.G.2    Simianu, M.C.3    Sykora, M.4    Kincaid, J.R.5    Sligar, S.G.6
  • 20
    • 34249044773 scopus 로고    scopus 로고
    • Mak, P. J., Denisov, I. G., Victoria, D., Makris, T. M., Deng, T.-J., Sligar, S. G., and Kincaid, J. R. (2007) Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle. J. Am. Chem. Soc. 129, 6382-6383.
    • Mak, P. J., Denisov, I. G., Victoria, D., Makris, T. M., Deng, T.-J., Sligar, S. G., and Kincaid, J. R. (2007) Resonance Raman Detection of the Hydroperoxo Intermediate in the Cytochrome P450 Enzymatic Cycle. J. Am. Chem. Soc. 129, 6382-6383.
  • 21
    • 0023915945 scopus 로고
    • Surface enhanced resonance Raman study of phenobarbital-induced rabbit liver cytochrome P-450 LM2
    • Hildebrandt, P., Greinert, R., Stier, A., Stockburger, M., and Taniguchi, H. (1988) Surface enhanced resonance Raman study of phenobarbital-induced rabbit liver cytochrome P-450 LM2. FEBS Lett. 227, 76-80.
    • (1988) FEBS Lett , vol.227 , pp. 76-80
    • Hildebrandt, P.1    Greinert, R.2    Stier, A.3    Stockburger, M.4    Taniguchi, H.5
  • 22
    • 0023753922 scopus 로고
    • Resonance Raman study of the cytochrome P-450 LM2-halothane intermediate complex
    • Hildebrandt, P., Garda, H., Stier, A., Stockburger, M., and Van Dyke, R. A. (1988) Resonance Raman study of the cytochrome P-450 LM2-halothane intermediate complex. FEBS Lett. 237, 15-20.
    • (1988) FEBS Lett , vol.237 , pp. 15-20
    • Hildebrandt, P.1    Garda, H.2    Stier, A.3    Stockburger, M.4    Van Dyke, R.A.5
  • 23
    • 0024852008 scopus 로고
    • Resonance Raman study on the structure of the active sites of microsomal cytochrome P-450 isozymes LM2 and LM4
    • Hildebrandt, P., Greinert, R., Stier, A., and Taniguchi, H. (1989) Resonance Raman study on the structure of the active sites of microsomal cytochrome P-450 isozymes LM2 and LM4. Eur. J. Biochem./FEBS 186, 291-302.
    • (1989) Eur. J. Biochem./FEBS , vol.186 , pp. 291-302
    • Hildebrandt, P.1    Greinert, R.2    Stier, A.3    Taniguchi, H.4
  • 24
    • 0024833499 scopus 로고
    • Protein-protein interactions in microsomal cytochrome P-450 isozyme LM2 and their effect on substrate binding
    • Hildebrandt, P., Garda, H., Stier, A., Bachmanova, G. I., Kanaeva, I. P., and Archakov, A. I. (1989) Protein-protein interactions in microsomal cytochrome P-450 isozyme LM2 and their effect on substrate binding. Eur. J. Biochem./FEBS 186, 383-388.
    • (1989) Eur. J. Biochem./FEBS , vol.186 , pp. 383-388
    • Hildebrandt, P.1    Garda, H.2    Stier, A.3    Bachmanova, G.I.4    Kanaeva, I.P.5    Archakov, A.I.6
  • 25
    • 0028138513 scopus 로고
    • Conformational analysis of mitochondrial and microsomal cytochrome P-450 by resonance Raman spectroscopy
    • Hildebrandt, P., Heibel, G., Anzenbacher, P., Lange, R., Kruger, V., and Stier, A. (1994) Conformational analysis of mitochondrial and microsomal cytochrome P-450 by resonance Raman spectroscopy. Biochemistry 33, 12920-12929.
    • (1994) Biochemistry , vol.33 , pp. 12920-12929
    • Hildebrandt, P.1    Heibel, G.2    Anzenbacher, P.3    Lange, R.4    Kruger, V.5    Stier, A.6
  • 26
    • 0030568828 scopus 로고    scopus 로고
    • Observation of structural variation and spin state conversion of cytochrome P450 CYP2B4 on binding of sterically different substrates
    • Macdonald, I. D. G., Smith, G. C. M., Graeme, C. M., Wolf, C. R., and Smith, W. E. (1996) Observation of structural variation and spin state conversion of cytochrome P450 CYP2B4 on binding of sterically different substrates. Biochem. Biophys. Res. Commun. 226, 51-58.
    • (1996) Biochem. Biophys. Res. Commun , vol.226 , pp. 51-58
    • Macdonald, I.D.G.1    Smith, G.C.M.2    Graeme, C.M.3    Wolf, C.R.4    Smith, W.E.5
  • 27
    • 0035965195 scopus 로고    scopus 로고
    • Elucidation of the differences between the 430- and 455-nm absorbing forms of P450-isocyanide adducts by resonance Raman spectroscopy
    • Tomita, T., Ogo, S., Egawa, T., Shimada, H., Okamoto, N., Imai, Y., Watanabe, Y., Ishimura, Y., and Kitagawa, T. (2001) Elucidation of the differences between the 430- and 455-nm absorbing forms of P450-isocyanide adducts by resonance Raman spectroscopy. J. Biol. Chem. 276, 36261-36267.
    • (2001) J. Biol. Chem , vol.276 , pp. 36261-36267
    • Tomita, T.1    Ogo, S.2    Egawa, T.3    Shimada, H.4    Okamoto, N.5    Imai, Y.6    Watanabe, Y.7    Ishimura, Y.8    Kitagawa, T.9
  • 28
    • 33646343223 scopus 로고    scopus 로고
    • Raman Evidence for Specific Substrate-Induced Structural Changes in the Heme Pocket of Human Cytochrome P450 Aromatase during the Three Consecutive Oxygen Activation Steps
    • Tosha, T., Kagawa, N., Ohta, T., Yoshioka, S., Waterman, M. R., and Kitagawa, T. (2006) Raman Evidence for Specific Substrate-Induced Structural Changes in the Heme Pocket of Human Cytochrome P450 Aromatase during the Three Consecutive Oxygen Activation Steps. Biochemistry 45, 5631-5640.
    • (2006) Biochemistry , vol.45 , pp. 5631-5640
    • Tosha, T.1    Kagawa, N.2    Ohta, T.3    Yoshioka, S.4    Waterman, M.R.5    Kitagawa, T.6
  • 30
    • 33645936665 scopus 로고    scopus 로고
    • Binding of bufuralol, dextromethorphan, and 3,4-methylene-dioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy
    • Bonifacio, A., Keizers, P. H. J., Commandeur, J. N. M., Vermeulen, N. P. E., Robert, B., Gooijer, C., and Van der Zwan, G. (2006) Binding of bufuralol, dextromethorphan, and 3,4-methylene-dioxymethylamphetamine to wild-type and F120A mutant cytochrome P450 2D6 studied by resonance Raman spectroscopy. Biochem. Biophys. Res. Commun. 343, 772-779.
    • (2006) Biochem. Biophys. Res. Commun , vol.343 , pp. 772-779
    • Bonifacio, A.1    Keizers, P.H.J.2    Commandeur, J.N.M.3    Vermeulen, N.P.E.4    Robert, B.5    Gooijer, C.6    Van der Zwan, G.7
  • 31
    • 0026702413 scopus 로고
    • Effects of cholesterol side-chain groups and adrenodoxin binding on the vibrational modes of carbon monoxide bound to cytochrome P-450scc: Implications of the productive and nonproductive substrate bindings
    • Tsubaki, M., Yoshikawa, S., Ichikawa, Y., and Yu, N.-T. (1992) Effects of cholesterol side-chain groups and adrenodoxin binding on the vibrational modes of carbon monoxide bound to cytochrome P-450scc: implications of the productive and nonproductive substrate bindings. Biochemistry 31, 8991-8999.
    • (1992) Biochemistry , vol.31 , pp. 8991-8999
    • Tsubaki, M.1    Yoshikawa, S.2    Ichikawa, Y.3    Yu, N.-T.4
  • 32
    • 0017170343 scopus 로고
    • Coupling of spin, substrate, and redox equilibria in cytochrome P450
    • Sligar, S. G. (1976) Coupling of spin, substrate, and redox equilibria in cytochrome P450. Biochemistry 15, 5399-5406.
    • (1976) Biochemistry , vol.15 , pp. 5399-5406
    • Sligar, S.G.1
  • 34
    • 0037065667 scopus 로고    scopus 로고
    • Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: Kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy
    • Matsunaga, I., Yamada, A., Lee, D.-S., Obayashi, E., Fujiwara, N., Kobayashi, K., Ogura, H., and Shiro, Y. (2002) Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy. Biochemistry 41, 1886-1892.
    • (2002) Biochemistry , vol.41 , pp. 1886-1892
    • Matsunaga, I.1    Yamada, A.2    Lee, D.-S.3    Obayashi, E.4    Fujiwara, N.5    Kobayashi, K.6    Ogura, H.7    Shiro, Y.8
  • 35
    • 0033550059 scopus 로고    scopus 로고
    • Resonance Raman Studies of Cytochrome P450BM3 and Its Complexes with Exogenous Ligands
    • Deng, T.-J., Proniewicz, L. M., Kincaid, J. R., Yeom, H., Macdonald, I. D. G., and Sligar, S. G. (1999) Resonance Raman Studies of Cytochrome P450BM3 and Its Complexes with Exogenous Ligands. Biochemistry 38, 13699-13706.
    • (1999) Biochemistry , vol.38 , pp. 13699-13706
    • Deng, T.-J.1    Proniewicz, L.M.2    Kincaid, J.R.3    Yeom, H.4    Macdonald, I.D.G.5    Sligar, S.G.6
  • 36
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • Miroux, B., and Walker, J. E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J. Mol. Biol. 260, 289-298.
    • (1996) J. Mol. Biol , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 38
    • 0024518203 scopus 로고
    • Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis
    • Shen, A. L., Porter, T. D., Wilson, T. E., and Kasper, C. B. (1989) Structural analysis of the FMN binding domain of NADPH-cytochrome P-450 oxidoreductase by site-directed mutagenesis. J. Biol. Chem. 264, 7584-7589.
    • (1989) J. Biol. Chem , vol.264 , pp. 7584-7589
    • Shen, A.L.1    Porter, T.D.2    Wilson, T.E.3    Kasper, C.B.4
  • 41
    • 50449100139 scopus 로고
    • J. Biol. Chem. 239
    • The carbon monoxide-binding pigment of liver microsomes. II
    • Omura, T., and Sato, R. (1964) The carbon monoxide-binding pigment of liver microsomes. II. Solubilization, purification, and properties. J. Biol. Chem. 239, 2379-2385.
    • (1964) , pp. 2379-2385
    • Omura, T.1    Sato, R.2
  • 42
    • 0017801794 scopus 로고
    • Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states
    • Vermilion, J. L., and Coon, M. J. (1978) Purified liver microsomal NADPH-cytochrome P-450 reductase. Spectral characterization of oxidation-reduction states. J. Biol. Chem. 253, 2694-2704.
    • (1978) J. Biol. Chem , vol.253 , pp. 2694-2704
    • Vermilion, J.L.1    Coon, M.J.2
  • 43
    • 0017869007 scopus 로고
    • The measurement of difference spectra: Application to the cytochromes of microsomes
    • Estabrook, R. W., and Werringloer, J. (1978) The measurement of difference spectra: application to the cytochromes of microsomes. Methods Enzymol. 52, 212-220.
    • (1978) Methods Enzymol , vol.52 , pp. 212-220
    • Estabrook, R.W.1    Werringloer, J.2
  • 45
    • 33845183059 scopus 로고
    • Consistent porphyrin force field. 3. Out-of-plane modes in the resonance Raman spectra of planar and ruffled nickel octaethylporphyrin
    • Li, X.-Y., Czernuszewicz, R. S., Kincaid, J. R., and Spiro, T. G. (1989) Consistent porphyrin force field. 3. Out-of-plane modes in the resonance Raman spectra of planar and ruffled nickel octaethylporphyrin. J. Am. Chem. Soc. 111, 7012-7023.
    • (1989) J. Am. Chem. Soc , vol.111 , pp. 7012-7023
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Spiro, T.G.4
  • 46
    • 0003096407 scopus 로고
    • Consistent porphyrin force field. 2. Nickel octaethylporphyrin skeletal and substituent mode assignments from nitrogen-15, meso-d4, and methylene-d16 Raman and infrared isotope shifts
    • Li, X.-Y., Czernuszewicz, R. S., Kincaid, J. R., Stein, P., and Spiro, T. G. (1990) Consistent porphyrin force field. 2. Nickel octaethylporphyrin skeletal and substituent mode assignments from nitrogen-15, meso-d4, and methylene-d16 Raman and infrared isotope shifts. J. Phys. Chem. 94, 47-61.
    • (1990) J. Phys. Chem , vol.94 , pp. 47-61
    • Li, X.-Y.1    Czernuszewicz, R.S.2    Kincaid, J.R.3    Stein, P.4    Spiro, T.G.5
  • 47
    • 0141988883 scopus 로고    scopus 로고
    • Determination of the Rate of Reduction of Oxyferrous Cytochrome P450 2B4 by 5-Deazariboflavin Adenine Dinucleotide T491V Cytochrome P450 Reductase
    • Zhang, H., Gruenke, L., Arscott, D., Harris, D. L., Glavanovich, M., Johnson, R., and Waskell, L. A. (2003) Determination of the Rate of Reduction of Oxyferrous Cytochrome P450 2B4 by 5-Deazariboflavin Adenine Dinucleotide T491V Cytochrome P450 Reductase. Biochemistry 42, 11594-11603.
    • (2003) Biochemistry , vol.42 , pp. 11594-11603
    • Zhang, H.1    Gruenke, L.2    Arscott, D.3    Harris, D.L.4    Glavanovich, M.5    Johnson, R.6    Waskell, L.A.7
  • 48
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin
    • Hu, S., Smith, K. M., and Spiro, T. G. (1996) Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin. J. Am. Chem. Soc. 118, 12638-12646.
    • (1996) J. Am. Chem. Soc , vol.118 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 49
    • 7044247187 scopus 로고    scopus 로고
    • Effects of Systematic Peripheral Group Deuteration on the Low-Frequency Resonance Raman Spectra of Myoglobin Derivatives
    • Mak, P. J., Podstawka, E., Kincaid, J. R., and Proniewicz, L. M. (2004) Effects of Systematic Peripheral Group Deuteration on the Low-Frequency Resonance Raman Spectra of Myoglobin Derivatives. Biopolymers 75, 217-228.
    • (2004) Biopolymers , vol.75 , pp. 217-228
    • Mak, P.J.1    Podstawka, E.2    Kincaid, J.R.3    Proniewicz, L.M.4
  • 50
    • 0027818118 scopus 로고
    • Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes
    • Hu, S., Morris, I. K., Singh, J. P., Smith, K. M., and Spiro, T. G. (1993) Complete assignment of cytochrome c resonance Raman spectra via enzymic reconstitution with isotopically labeled hemes. J. Am. Chem. Soc. 115, 12446-12458.
    • (1993) J. Am. Chem. Soc , vol.115 , pp. 12446-12458
    • Hu, S.1    Morris, I.K.2    Singh, J.P.3    Smith, K.M.4    Spiro, T.G.5
  • 53
    • 0019321102 scopus 로고
    • Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system
    • French, J. S., Guengerich, F. P., and Coon, M. J. (1980) Interactions of cytochrome P-450, NADPH-cytochrome P-450 reductase, phospholipid, and substrate in the reconstituted liver microsomal enzyme system. J. Biol. Chem. 255, 4112-4119.
    • (1980) J. Biol. Chem , vol.255 , pp. 4112-4119
    • French, J.S.1    Guengerich, F.P.2    Coon, M.J.3
  • 54
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • Hasemann, C. A., Kurumbail, R. G., Boddupalli, S. S., Peterson, J. A., 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. 41-62
    • Hasemann, C.A.1    Kurumbail, R.G.2    Boddupalli, S.S.3    Peterson, J.A.4    Deisenhofer, J.5
  • 55
    • 0030891287 scopus 로고    scopus 로고
    • Interactions between substrate analogues and heme ligands in nitric oxide synthase
    • Wang, J., Stuehr, D. J., and Rousseau, D. L. (1997) Interactions between substrate analogues and heme ligands in nitric oxide synthase. Biochemistry 36, 4595-4606.
    • (1997) Biochemistry , vol.36 , pp. 4595-4606
    • Wang, J.1    Stuehr, D.J.2    Rousseau, D.L.3
  • 56
    • 0001314340 scopus 로고    scopus 로고
    • Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes
    • Smulevich, G., Hu, S., Rodgers, K. R., Goodin, D. B., Smith, K. M., and Spiro, T. G. (1996) Heme-protein interactions in cytochrome c peroxidase revealed by site-directed mutagenesis and resonance Raman spectra of isotopically labeled hemes. Biospectroscopy 2, 365-376.
    • (1996) Biospectroscopy , vol.2 , pp. 365-376
    • Smulevich, G.1    Hu, S.2    Rodgers, K.R.3    Goodin, D.B.4    Smith, K.M.5    Spiro, T.G.6
  • 57
    • 3042553224 scopus 로고    scopus 로고
    • Structure of Mammalian Cytochrome P450 2B4 Complexed with 4-(4-Chlorophenyl)imidazole at 1.9-Å Resolution: Insight into the Range of P450 Conformations and the Coordination of Redox
    • Scott, E. E., White, M. A., He, Y. A., Johnson, E. F., Stout, C. D., and Halpert, J. R. (2004) Structure of Mammalian Cytochrome P450 2B4 Complexed with 4-(4-Chlorophenyl)imidazole at 1.9-Å Resolution: Insight into the Range of P450 Conformations and the Coordination of Redox. J. Biol. Chem. 279, 27294-27301.
    • (2004) J. Biol. Chem , vol.279 , pp. 27294-27301
    • Scott, E.E.1    White, M.A.2    He, Y.A.3    Johnson, E.F.4    Stout, C.D.5    Halpert, J.R.6
  • 58
    • 33646854265 scopus 로고    scopus 로고
    • Structure of Microsomal Cytochrome P450 2B4 Complexed with the Antifungal Drug Bifonazole: Insight into P450 conformational plasticity and membrane interaction
    • Zhao, Y., White, M. A., Muralidhara, B. K., Sun, L., Halpert, J. R., and Stout, C. D. (2006) Structure of Microsomal Cytochrome P450 2B4 Complexed with the Antifungal Drug Bifonazole: insight into P450 conformational plasticity and membrane interaction. J. Biol. Chem. 281, 5973-5981.
    • (2006) J. Biol. Chem , vol.281 , pp. 5973-5981
    • Zhao, Y.1    White, M.A.2    Muralidhara, B.K.3    Sun, L.4    Halpert, J.R.5    Stout, C.D.6
  • 59
    • 0242386453 scopus 로고    scopus 로고
    • Relationship between heme vinyl conformation and the protein matrix in peroxidases
    • Marzocchi, M. P., and Smulevich, G. (2003) Relationship between heme vinyl conformation and the protein matrix in peroxidases. J. Raman Spectrosc. 34, 725-736.
    • (2003) J. Raman Spectrosc , vol.34 , pp. 725-736
    • Marzocchi, M.P.1    Smulevich, G.2
  • 62
    • 0037169558 scopus 로고    scopus 로고
    • Complex formation of cytochrome P450cam with putidaredoxin. Ecidence for protein-specific interactions involving the proximal thiolate ligand
    • Unno, M., Christian, J. F., Sjodin, T., Benson, D. E., Macdonald, I. D. G., Sligar, S. G., and Champion, P. M. (2002) Complex formation of cytochrome P450cam with putidaredoxin. Ecidence for protein-specific interactions involving the proximal thiolate ligand. J. Biol. Chem. 277, 2547-2553.
    • (2002) J. Biol. Chem , vol.277 , pp. 2547-2553
    • Unno, M.1    Christian, J.F.2    Sjodin, T.3    Benson, D.E.4    Macdonald, I.D.G.5    Sligar, S.G.6    Champion, P.M.7
  • 63
    • 0035925164 scopus 로고    scopus 로고
    • Hydroxylation of Camphor by Reduced Oxy-Cytochrome P450cam: Mechanistic Implications of EPR and ENDOR Studies of Catalytic Intermediates in Native and Mutant Enzymes
    • Davydov, R., Makris, T. M., Kofman, V., Werst, D. E., Sligar, S. G., and Hoffman, B. M. (2001) Hydroxylation of Camphor by Reduced Oxy-Cytochrome P450cam: Mechanistic Implications of EPR and ENDOR Studies of Catalytic Intermediates in Native and Mutant Enzymes. J. Am. Chem. Soc. 123, 1403-1415.
    • (2001) J. Am. Chem. Soc , vol.123 , pp. 1403-1415
    • Davydov, R.1    Makris, T.M.2    Kofman, V.3    Werst, D.E.4    Sligar, S.G.5    Hoffman, B.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.