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Volumn 344, Issue 2, 2004, Pages 455-469

Conformational states of cytochrome P450cam revealed by trapping of synthetic molecular wires

Author keywords

cytochrome P450; molecular wires; sensitizer linked substrates; substrate recognition; X ray crystallography

Indexed keywords

ADAMANTANE DERIVATIVE; ALKANE DERIVATIVE; CAMPHOR; CYTOCHROME P450; DANSYL CHLORIDE; THREONINE; WATER;

EID: 7444264562     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.09.046     Document Type: Article
Times cited : (50)

References (73)
  • 1
    • 0037069410 scopus 로고    scopus 로고
    • Impact of enzyme motion on activity
    • S. Hammes-Schiffer Impact of enzyme motion on activity Biochemistry 41 2002 13335 13343
    • (2002) Biochemistry , vol.41 , pp. 13335-13343
    • Hammes-Schiffer, S.1
  • 3
    • 0033200309 scopus 로고    scopus 로고
    • How similar are P450s and what can their differences teach us?
    • S.E. Graham, and J.A. Peterson How similar are P450s and what can their differences teach us? Arch. Biochem. Biophys. 369 1999 24 29
    • (1999) Arch. Biochem. Biophys. , vol.369 , pp. 24-29
    • Graham, S.E.1    Peterson, J.A.2
  • 5
    • 0032039678 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenases
    • L.-L. Wong Cytochrome P450 monooxygenases Curr. Opin. Chem. Biol. 2 1998 263 268
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 263-268
    • Wong, L.-L.1
  • 6
    • 0035750366 scopus 로고    scopus 로고
    • Recent advances in P450 research
    • J.L. Raucy, and S.W. Allen Recent advances in P450 research Pharmacogenom. J. 1 2001 178 186
    • (2001) Pharmacogenom. J. , vol.1 , pp. 178-186
    • Raucy, J.L.1    Allen, S.W.2
  • 7
    • 0036560522 scopus 로고    scopus 로고
    • Cytochrome P450 enzymes in the generation of commercial products
    • F.P. Guengerich Cytochrome P450 enzymes in the generation of commercial products Nature Rev. Drug Discov. 1 2002 359 366
    • (2002) Nature Rev. Drug Discov. , vol.1 , pp. 359-366
    • Guengerich, F.P.1
  • 9
    • 0034724310 scopus 로고    scopus 로고
    • Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity
    • J.A.R. Cupp-Vickery, and Z. Hatziris Crystal structures of ligand complexes of P450eryF exhibiting homotropic cooperativity Proc. Natl Acad. Sci. USA 97 2000 3050 3055
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 3050-3055
    • Cupp-Vickery, J.A.R.1    Hatziris, Z.2
  • 10
    • 0034108229 scopus 로고    scopus 로고
    • Dual role of human cytochrome P450 3A4 residue Phe-304 in substrate specificity and cooperativity
    • T.L. Domanski, Y.A. He, G.R. Harlow, and J.R. Halpert Dual role of human cytochrome P450 3A4 residue Phe-304 in substrate specificity and cooperativity J. Pharmacol. Expt. Ther. 293 2000 585 591
    • (2000) J. Pharmacol. Expt. Ther. , vol.293 , pp. 585-591
    • Domanski, T.L.1    He, Y.A.2    Harlow, G.R.3    Halpert, J.R.4
  • 11
    • 0034705191 scopus 로고    scopus 로고
    • Elucidation of distinct ligand binding sites for cytochrome P450 3A4
    • N.A. Hosea, G.P. Miller, and R.P. Guengerich Elucidation of distinct ligand binding sites for cytochrome P450 3A4 Biochemistry 39 2000 5929 5939
    • (2000) Biochemistry , vol.39 , pp. 5929-5939
    • Hosea, N.A.1    Miller, G.P.2    Guengerich, R.P.3
  • 12
    • 0034956877 scopus 로고    scopus 로고
    • Dapsone activation of CYP2C9-mediated metabolism: Evidence for activation of multiple substrates and a two-site model
    • J.M. Hutzler, M.J. Hauer, and T.S. Tracy Dapsone activation of CYP2C9-mediated metabolism: evidence for activation of multiple substrates and a two-site model Drug Metab. Dispos. 29 2001 1029 1034
    • (2001) Drug Metab. Dispos. , vol.29 , pp. 1029-1034
    • Hutzler, J.M.1    Hauer, M.J.2    Tracy, T.S.3
  • 13
    • 0034976635 scopus 로고    scopus 로고
    • Heterotropic Cooperativity of Cytochrome P450 3A4 and Potential Drug-Drug Interactions
    • W. Tang, and R.A. Stearns Heterotropic Cooperativity of Cytochrome P450 3A4 and Potential Drug-Drug Interactions Curr. Drug Metab. 2 2001 185 198
    • (2001) Curr. Drug Metab. , vol.2 , pp. 185-198
    • Tang, W.1    Stearns, R.A.2
  • 14
    • 0037048522 scopus 로고    scopus 로고
    • Pyrene·pyrene complexes at the active site of cytochrome P450 3A4: Evidence for a multiple substrate binding site
    • M.J. Dabrowski, M.L. Schrag, L.C. Wienkers, and W.M. Atkins Pyrene·pyrene complexes at the active site of cytochrome P450 3A4: evidence for a multiple substrate binding site J. Am. Chem. Soc. 124 2002 11866 11867
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11866-11867
    • Dabrowski, M.J.1    Schrag, M.L.2    Wienkers, L.C.3    Atkins, W.M.4
  • 16
    • 0037672866 scopus 로고    scopus 로고
    • Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 Å resolution: Evidence for multiple substrate binding modes
    • M.R. Wester, E.F. Johnson, C. Marques-Soares, P.M. Dansette, D. Mansuy, and C.D. Stout Structure of a substrate complex of mammalian cytochrome P450 2C5 at 2.3 Å resolution: evidence for multiple substrate binding modes Biochemistry 42 2003 6370 6379
    • (2003) Biochemistry , vol.42 , pp. 6370-6379
    • Wester, M.R.1    Johnson, E.F.2    Marques-Soares, C.3    Dansette, P.M.4    Mansuy, D.5    Stout, C.D.6
  • 17
    • 0029170124 scopus 로고
    • Prediction of regiospecific hydroxylation of camphor analogs by cytochrome P450cam
    • D. Harris, and G. Loew Prediction of regiospecific hydroxylation of camphor analogs by cytochrome P450cam J. Am. Chem. Soc. 117 1995 2738 2746
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2738-2746
    • Harris, D.1    Loew, G.2
  • 18
    • 0034739054 scopus 로고    scopus 로고
    • Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam
    • B. Das, V. Helms, V. Lounnas, and R.C. Wade Multicopy molecular dynamics simulations suggest how to reconcile crystallographic and product formation data for camphor enantiomers bound to cytochrome P-450cam J. Inorg. Biochem. 81 2000 121 131
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 121-131
    • Das, B.1    Helms, V.2    Lounnas, V.3    Wade, R.C.4
  • 19
    • 0033616138 scopus 로고    scopus 로고
    • Forty years of cytochrome P450
    • T. Omura Forty years of cytochrome P450 Biochem. Biophys. Res. Commun. 266 1999 690 698
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 690-698
    • Omura, T.1
  • 20
    • 0033970047 scopus 로고    scopus 로고
    • Mammalian microsomal cytochrome P450 monooxygenase: Structural adaptations for membrane binding and functional diversity
    • P.A. Williams, J. Cosme, V. Sridhar, E.F. Johnson, and D.E. McRee Mammalian microsomal cytochrome P450 monooxygenase: structural adaptations for membrane binding and functional diversity Mol. Cell 5 2000 121 131
    • (2000) Mol. Cell , vol.5 , pp. 121-131
    • Williams, P.A.1    Cosme, J.2    Sridhar, V.3    Johnson, E.F.4    McRee, D.E.5
  • 22
    • 0029643786 scopus 로고
    • Structure and function of cytochromes P450: A comparative analysis of three crystal structures
    • C.A. Hasemann, R.G. Kurumbail, S.S. Boddupalli, J.A. Peterson, and J. Deisenhofer Structure and function of cytochromes P450: a comparative analysis of three crystal structures Structure 3 1995 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
  • 23
    • 0022919721 scopus 로고
    • Crystal structure of substrate-free Pseudomonas putida cytochrome P-450
    • T.L. Poulos, B.C. Finzel, and A.J. Howard Crystal structure of substrate-free Pseudomonas putida cytochrome P-450 Biochemistry 25 1986 5314 5322
    • (1986) Biochemistry , vol.25 , pp. 5314-5322
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 24
    • 0023645035 scopus 로고
    • High resolution crystal structure of cytochrome P450cam
    • T.L. Poulos, B.C. Finzel, and A.J. Howard High resolution crystal structure of cytochrome P450cam J. Mol. Biol. 195 1987 687 700
    • (1987) J. Mol. Biol. , vol.195 , pp. 687-700
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 25
    • 0024208742 scopus 로고
    • The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis
    • W.M. Atkins, and S.G. Sligar The roles of active site hydrogen bonding in cytochrome P-450cam as revealed by site-directed mutagenesis J. Biol. Chem. 263 1988 18842 18849
    • (1988) J. Biol. Chem. , vol.263 , pp. 18842-18849
    • Atkins, W.M.1    Sligar, S.G.2
  • 26
    • 0024566973 scopus 로고
    • Molecular recognition in cyt P450: Alteration of regioselective alkane hydroxylation via protein engineering
    • W.M. Atkins, and S.G. Sligar Molecular recognition in cyt P450: alteration of regioselective alkane hydroxylation via protein engineering J. Am. Chem. Soc. 111 1989 2715
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 2715
    • Atkins, W.M.1    Sligar, S.G.2
  • 27
    • 0024579824 scopus 로고
    • The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM
    • R. Raag, and T.L. Poulos The structural basis for substrate-induced changes in redox potential and spin equilibrium in cytochrome P-450CAM Biochemistry 28 1989 917 922
    • (1989) Biochemistry , vol.28 , pp. 917-922
    • Raag, R.1    Poulos, T.L.2
  • 28
    • 0025761693 scopus 로고
    • Crystal structures of cytochrome-P-450CAM complexed with camphane thiocamphor, and adamantane-factors controlling P-450 substrate hydroxylation
    • R. Raag, and T.L. Poulos Crystal structures of cytochrome-P-450CAM complexed with camphane thiocamphor, and adamantane-factors controlling P-450 substrate hydroxylation Biochemistry 30 1991 2674 2684
    • (1991) Biochemistry , vol.30 , pp. 2674-2684
    • Raag, R.1    Poulos, T.L.2
  • 29
    • 0027258737 scopus 로고
    • Inhibitor-induced conformational change in cytochrome P-450CAM
    • R. Raag, H. Li, B.C. Jones, and T.L. Poulos Inhibitor-induced conformational change in cytochrome P-450CAM Biochemistry 32 1993 4571 4578
    • (1993) Biochemistry , vol.32 , pp. 4571-4578
    • Raag, R.1    Li, H.2    Jones, B.C.3    Poulos, T.L.4
  • 30
    • 0030040103 scopus 로고    scopus 로고
    • Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket
    • V. Helms, E. Deprez, E. Gill, C. Barret, G.H.B. Hoa, and R.C. Wade Improved binding of cytochrome P450cam substrate analogues designed to fill extra space in the substrate binding pocket Biochemistry 35 1996 1485 1499
    • (1996) Biochemistry , vol.35 , pp. 1485-1499
    • Helms, V.1    Deprez, E.2    Gill, E.3    Barret, C.4    Hoa, G.H.B.5    Wade, R.C.6
  • 31
    • 0032523238 scopus 로고    scopus 로고
    • Cytochrome P450cam substrate specificity: Relationship between structure and catalytic oxidation of alkylbenzenes
    • O. Sibbesen, Z. Zhang, and P.R. Ortiz de Montellano Cytochrome P450cam substrate specificity: relationship between structure and catalytic oxidation of alkylbenzenes Arch. Biochem. Biophys. 353 1998 285 296
    • (1998) Arch. Biochem. Biophys. , vol.353 , pp. 285-296
    • Sibbesen, O.1    Zhang, Z.2    Ortiz De Montellano, P.R.3
  • 32
    • 0037171134 scopus 로고    scopus 로고
    • Cytochrome P-450-CO and substrates: Lessons from ligand binding under high pressure
    • C. Jung Cytochrome P-450-CO and substrates: lessons from ligand binding under high pressure Biochim. Biophys. Acta 1595 2002 309 328
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 309-328
    • Jung, C.1
  • 33
    • 0026683129 scopus 로고
    • Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome-P450 and cytochrome-P420
    • A.V. Wells, P.S. Li, P.M. Champion, S.A. Martinis, and S.G. Sligar Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome-P450 and cytochrome-P420 Biochemistry 31 1992 4384 4393
    • (1992) Biochemistry , vol.31 , pp. 4384-4393
    • Wells, A.V.1    Li, P.S.2    Champion, P.M.3    Martinis, S.A.4    Sligar, S.G.5
  • 34
    • 0027174076 scopus 로고
    • Conformational dynamics of cytochrome P450cam as monitored by photoacoustic calorimetry
    • C. DiPrimo, G.H.B. Hoa, E. Deprez, P. Douzou, and S.G. Sligar Conformational dynamics of cytochrome P450cam as monitored by photoacoustic calorimetry Biochemistry 32 1993 3671 3676
    • (1993) Biochemistry , vol.32 , pp. 3671-3676
    • Diprimo, C.1    Hoa, G.H.B.2    Deprez, E.3    Douzou, P.4    Sligar, S.G.5
  • 35
    • 0037058831 scopus 로고    scopus 로고
    • Role of protein and substrate dynamics in catalysis by Pseudomonas putida cytochrome P450cam
    • S. Prasad, and S. Mitra Role of protein and substrate dynamics in catalysis by Pseudomonas putida cytochrome P450cam Biochemistry 41 2002 14499 14508
    • (2002) Biochemistry , vol.41 , pp. 14499-14508
    • Prasad, S.1    Mitra, S.2
  • 36
    • 0034634391 scopus 로고    scopus 로고
    • How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways
    • S.K. Ludemann, V. Lounnas, and R.C. Wade How do substrates enter and products exit the buried active site of cytochrome P450cam? 2. Steered molecular dynamics and adiabatic mapping of substrate pathways J. Mol. Biol. 303 2000 813 830
    • (2000) J. Mol. Biol. , vol.303 , pp. 813-830
    • Ludemann, S.K.1    Lounnas, V.2    Wade, R.C.3
  • 37
    • 0034634393 scopus 로고    scopus 로고
    • How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms
    • S.K. Ludemann, V. Lounnas, and R.C. Wade How do substrates enter and products exit the buried active site of cytochrome P450cam? 1. Random expulsion molecular dynamics investigation of ligand access channels and mechanisms J. Mol. Biol. 303 2000 797 811
    • (2000) J. Mol. Biol. , vol.303 , pp. 797-811
    • Ludemann, S.K.1    Lounnas, V.2    Wade, R.C.3
  • 38
    • 0030917740 scopus 로고    scopus 로고
    • Exceptionally stable salt bridges in cytochrome P450cam have functional roles
    • V. Lounnas, and R.C. Wade Exceptionally stable salt bridges in cytochrome P450cam have functional roles Biochemistry 36 1997 5402 5417
    • (1997) Biochemistry , vol.36 , pp. 5402-5417
    • Lounnas, V.1    Wade, R.C.2
  • 40
    • 0035853108 scopus 로고    scopus 로고
    • Crystal structure of cytochrome P450 14 alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors
    • L.M. Podust, T.L. Poulos, and M.R. Waterman Crystal structure of cytochrome P450 14 alpha-sterol demethylase (CYP51) from Mycobacterium tuberculosis in complex with azole inhibitors Proc. Natl Acad. Sci. USA 98 2001 3068 3073
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3068-3073
    • Podust, L.M.1    Poulos, T.L.2    Waterman, M.R.3
  • 41
    • 0037809271 scopus 로고    scopus 로고
    • The 1.92 Å structure of Streptomyces coelicolor A3(2) CYP154C1: A new monooxygenase that functionalizes macrolide ring systems
    • L. Podust, Y. Kim, M. Arase, B.A. Neely, B.J. Beck, and H. Bach The 1.92 Å structure of Streptomyces coelicolor A3(2) CYP154C1: a new monooxygenase that functionalizes macrolide ring systems J. Biol. Chem. 278 2003 12214 12221
    • (2003) J. Biol. Chem. , vol.278 , pp. 12214-12221
    • Podust, L.1    Kim, Y.2    Arase, M.3    Neely, B.A.4    Beck, B.J.5    Bach, H.6
  • 42
    • 0033555652 scopus 로고    scopus 로고
    • Substrates for rapid delivery of electrons and holes to buried active sites in proteins
    • J.J. Wilker, I.J. Dmochowski, J.H. Dawson, J.R. Winkler, and H.B. Gray Substrates for rapid delivery of electrons and holes to buried active sites in proteins Angewandte Chemie 38 1999 90 92
    • (1999) Angewandte Chemie , vol.38 , pp. 90-92
    • Wilker, J.J.1    Dmochowski, I.J.2    Dawson, J.H.3    Winkler, J.R.4    Gray, H.B.5
  • 47
    • 0026352457 scopus 로고
    • Crystal structure of the cytochrome-P-450CAM active site mutant Thr252Ala
    • R. Raag, S.A. Martinis, S.G. Sligar, and T.L. Poulos Crystal structure of the cytochrome-P-450CAM active site mutant Thr252Ala Biochemistry 30 1991 11420 11429
    • (1991) Biochemistry , vol.30 , pp. 11420-11429
    • Raag, R.1    Martinis, S.A.2    Sligar, S.G.3    Poulos, T.L.4
  • 48
    • 0036888353 scopus 로고    scopus 로고
    • Improvements in the analysis of domain motions in proteins from conformational change: DynDom verison 1.50
    • S. Hayward, and R.A. Lee Improvements in the analysis of domain motions in proteins from conformational change: DynDom verison 1.50 J. Mol. Graph. Model. 21 2002 181 183
    • (2002) J. Mol. Graph. Model. , vol.21 , pp. 181-183
    • Hayward, S.1    Lee, R.A.2
  • 49
    • 0032769661 scopus 로고    scopus 로고
    • Structural principles governing domain motions in proteins
    • S. Hayward Structural principles governing domain motions in proteins Proteins: Struct. Funct. Genet. 36 1999 425 435
    • (1999) Proteins: Struct. Funct. Genet. , vol.36 , pp. 425-435
    • Hayward, S.1
  • 50
    • 0024579824 scopus 로고
    • The structural basis for substrate induced changes in redox potential and spin equilibrium in P-450cam
    • R. Raag, and T.L. Poulos The structural basis for substrate induced changes in redox potential and spin equilibrium in P-450cam Biochemistry 28 1989 917 922
    • (1989) Biochemistry , vol.28 , pp. 917-922
    • Raag, R.1    Poulos, T.L.2
  • 51
    • 0021832318 scopus 로고
    • High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria
    • M.T. Fisher, S.F. Scarlata, and S.G. Sligar High-pressure investigations of cytochrome P-450 spin and substrate binding equilibria Arch. Biochem. Biophys. 240 1985 456 463
    • (1985) Arch. Biochem. Biophys. , vol.240 , pp. 456-463
    • Fisher, M.T.1    Scarlata, S.F.2    Sligar, S.G.3
  • 52
    • 0032515405 scopus 로고    scopus 로고
    • Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein
    • K. Di Gleria, D.P. Nickerson, H.A.O. Hill, L.-L. Wong, and V. Fulop Covalent attachment of an electroactive sulfydryl reagent in the active site of cytochrome P450cam as revealed by the crystal structure of the modified protein J. Am. Chem. Soc. 120 1998 46 52
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 46-52
    • Di Gleria, K.1    Nickerson, D.P.2    Hill, H.A.O.3    Wong, L.-L.4    Fulop, V.5
  • 53
    • 0032530836 scopus 로고    scopus 로고
    • A database of macromolecular motions
    • M. Gerstein, and W. Krebs A database of macromolecular motions Nucleic Acids Res. 26 1998 4280 4290
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4280-4290
    • Gerstein, M.1    Krebs, W.2
  • 54
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • S.J. Teague Implications of protein flexibility for drug discovery Nature Rev. Drug Discov. 2 2003 527 541
    • (2003) Nature Rev. Drug Discov. , vol.2 , pp. 527-541
    • Teague, S.J.1
  • 55
    • 0037436388 scopus 로고    scopus 로고
    • Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure
    • P. Akamine, Madhusudan, J. Wu, N.H. Xuong, L.F. Ten Eyck, and S.S. Taylor Dynamic features of cAMP-dependent protein kinase revealed by apoenzyme crystal structure J. Mol. Biol. 327 2003 159 171
    • (2003) J. Mol. Biol. , vol.327 , pp. 159-171
    • Akamine, P.1    Madhusudan2    Wu, J.3    Xuong, N.H.4    Ten Eyck, L.F.5    Taylor, S.S.6
  • 57
    • 0034698277 scopus 로고    scopus 로고
    • Binding of camphor to Psuedomonas putida cytochrome P450cam: Steady-state and picosecond time-resolved fluorescence studies
    • S. Prasad, S. Mazumdar, and S. Mitra Binding of camphor to Psuedomonas putida cytochrome P450cam: steady-state and picosecond time-resolved fluorescence studies FEBS Letters 477 2000 157 160
    • (2000) FEBS Letters , vol.477 , pp. 157-160
    • Prasad, S.1    Mazumdar, S.2    Mitra, S.3
  • 58
    • 0002782723 scopus 로고
    • Bacterial P450s: Structural similarities and functional differences
    • (Ortiz de Montellano, P. R., ed.), 2nd edit., Plenum Press, New York.
    • Peterson, J. A. & Graham-Lorence, S. E. (1995). Bacterial P450s: structural similarities and functional differences. In Cytochrome P450: Structure, Mechanism and Biochemistry (Ortiz de Montellano, P. R., ed.), 2nd edit., pp. 151-180, Plenum Press, New York.
    • (1995) Cytochrome P450: Structure, Mechanism and Biochemistry , pp. 151-180
    • Peterson, J.A.1    Graham-Lorence, S.E.2
  • 59
    • 0029876059 scopus 로고    scopus 로고
    • The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction
    • S. Modi, M.J. Sutcliffe, W.U. Primrose, L.Y. Lian, and G.C. Roberts The catalytic mechanism of cytochrome P450 BM3 involves a 6 Å movement of the bound substrate on reduction Nature Struct. Biol. 3 1996 414 417
    • (1996) Nature Struct. Biol. , vol.3 , pp. 414-417
    • Modi, S.1    Sutcliffe, M.J.2    Primrose, W.U.3    Lian, L.Y.4    Roberts, G.C.5
  • 60
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome p450BM-3 hemedomain complexed with the fatty acid substrate, palmitoleic acid
    • H. Li, and T.L. Poulos The structure of the cytochrome p450BM-3 hemedomain complexed with the fatty acid substrate, palmitoleic acid Nature Struct. Biol. 4 1997 140 146
    • (1997) Nature Struct. Biol. , vol.4 , pp. 140-146
    • Li, H.1    Poulos, T.L.2
  • 61
    • 0034613190 scopus 로고    scopus 로고
    • Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus
    • J.K. Yano, L.S. Koo, D.J. Schuller, H. Li, P.R.O. De Montellano, and T.L. Poulos Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus J. Biol. Chem. 275 2000 31086 31092
    • (2000) J. Biol. Chem. , vol.275 , pp. 31086-31092
    • Yano, J.K.1    Koo, L.S.2    Schuller, D.J.3    Li, H.4    De Montellano, P.R.O.5    Poulos, T.L.6
  • 62
    • 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 coordination of redox partner binding
    • E.E. Scott, M.A. White, Y.A. He, E.F. Johnson, C.D. Stout, and J.R. Halpert 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 coordination of redox partner binding J. Biol. Chem. 279 2004 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
  • 64
    • 0141925683 scopus 로고    scopus 로고
    • NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin
    • T. Tosha, S. Yoshioka, S. Takahashi, K. Ishimori, H. Shimada, and I. Morishima NMR study on the structural changes of cytochrome P450cam upon the complex formation with putidaredoxin J. Biol. Chem. 278 2003 39809 39821
    • (2003) J. Biol. Chem. , vol.278 , pp. 39809-39821
    • Tosha, T.1    Yoshioka, S.2    Takahashi, S.3    Ishimori, K.4    Shimada, H.5    Morishima, I.6
  • 65
    • 0034681279 scopus 로고    scopus 로고
    • Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Tropedo californica
    • G. Koellner, G. Kryger, C.B. Millard, I. Siman, J.L. Sussman, and T. Steiner Active-site gorge and buried water molecules in crystal structures of acetylcholinesterase from Tropedo californica J. Mol. Biol. 296 2000 713 726
    • (2000) J. Mol. Biol. , vol.296 , pp. 713-726
    • Koellner, G.1    Kryger, G.2    Millard, C.B.3    Siman, I.4    Sussman, J.L.5    Steiner, T.6
  • 66
    • 0026481153 scopus 로고
    • A critical role of protein-bound water in the catalytic cycle of cytochrome-P-450 camphor
    • C. Diprimo, S.G. Sligar, G.H.B. Hoa, and P. Douzou A critical role of protein-bound water in the catalytic cycle of cytochrome-P-450 camphor FEBS Letters 312 1992 252 254
    • (1992) FEBS Letters , vol.312 , pp. 252-254
    • Diprimo, C.1    Sligar, S.G.2    Hoa, G.H.B.3    Douzou, P.4
  • 67
    • 0032583439 scopus 로고    scopus 로고
    • Effects of ligation and folding on reduction potentials of heme proteins
    • F.A. Tezcan, J.R. Winkler, and H.B. Gray Effects of ligation and folding on reduction potentials of heme proteins J. Am. Chem. Soc. 120 1998 13383 13388
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13383-13388
    • Tezcan, F.A.1    Winkler, J.R.2    Gray, H.B.3
  • 68
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 70
    • 0032790081 scopus 로고    scopus 로고
    • XtalView Xfit-A versatile program for manipulating atomic coordinates and electron density
    • D.E. McRee XtalView Xfit-A versatile program for manipulating atomic coordinates and electron density J. Struct. Biol. 125 1999 156 165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 71
    • 0008921541 scopus 로고    scopus 로고
    • Least-squares refinement of macromolecules: Estimated standard deviations, NCS restraints and factors affecting convergence
    • E. Dodson M. Moore A. Ralph S. Bailey Daresbury Laboratory Warrington, UK
    • G.M. Sheldrick Least-squares refinement of macromolecules: estimated standard deviations, NCS restraints and factors affecting convergence E. Dodson M. Moore A. Ralph S. Bailey Proceedings of the CCP4 Study Weekend, January 1996 1996 Daresbury Laboratory Warrington, UK 47 58
    • (1996) Proceedings of the CCP4 Study Weekend, January 1996 , pp. 47-58
    • Sheldrick, G.M.1
  • 72
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • R.A. Laskowski, D.S. Moss, and J.M. Thornton Main-chain bond lengths and bond angles in protein structures J. Mol. Biol. 231 1993 1049 1067
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3


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