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Volumn , Issue , 2007, Pages 99-122

The Bacterial Cytochrome P450 Monooxygenases: P450cam and P450BM-3

Author keywords

Bacterial cytochrome P450 monooxygenases; Biotransformation by bacterial P450 enzymes; General features of P450BM 3; General features of P450cam; Modern biooxidation; Scope of P450 engineering

Indexed keywords


EID: 84888646739     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9783527611522.ch4     Document Type: Chapter
Times cited : (14)

References (92)
  • 2
    • 0041513426 scopus 로고    scopus 로고
    • Reactions catalyzed by bacterial cytochromes P 450
    • Cryle, M.J., Stok, J.E., De Voss, J.J. Reactions catalyzed by bacterial cytochromes P 450. Aust J Chem 2003, 56, 749.
    • (2003) Aust J Chem , vol.56 , pp. 749
    • Cryle, M.J.1    Stok, J.E.2    De Voss, J.J.3
  • 3
    • 0017831786 scopus 로고
    • Bacterial P450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase
    • Gunsalus, I.C., Wagner, G.C. Bacterial P450cam methylene monooxygenase components: Cytochrome m, putidaredoxin, and putidaredoxin reductase. Methods Enzymol 1978, 52, 166.
    • (1978) Methods Enzymol , vol.52 , pp. 166
    • Gunsalus, I.C.1    Wagner, G.C.2
  • 4
    • 0016738181 scopus 로고
    • w-1, w-2 and w-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium
    • Miura, Y., Fulco, A.J. w-1, w-2 and w-3 hydroxylation of long-chain fatty acids, amides and alcohols by a soluble enzyme system from Bacillus megaterium. Biochim Biophys Acta 1975, 388, 305.
    • (1975) Biochim Biophys Acta , vol.388 , pp. 305
    • Miura, Y.1    Fulco, A.J.2
  • 5
    • 0025922972 scopus 로고
    • P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation
    • Fulco, A.J. P450BM-3 and other inducible bacterial P450 cytochromes: biochemistry and regulation. Annu Rev Pharmacol Toxicol 1991, 31, 177.
    • (1991) Annu Rev Pharmacol Toxicol , vol.31 , pp. 177
    • Fulco, A.J.1
  • 6
    • 0003631066 scopus 로고    scopus 로고
    • Cytochrome P450: Structure, Mechanism, and Biochemistry
    • 3rd edn. New York: Kluwer Academic/Plenum Press
    • Ortiz de Montellano, P.R. (ed). Cytochrome P450: Structure, Mechanism, and Biochemistry, 3rd edn. New York: Kluwer Academic/Plenum Press, 2005.
    • (2005)
    • Ortiz De Montellano, P.R.1
  • 7
    • 0031691120 scopus 로고    scopus 로고
    • Biocatalyst engineering by assembly of fatty acid transport and oxidation activities for in vivo application of cytochrome P-450BM-3 monooxygenase
    • Schneider, S., Wubbolts, M.G., Sanglard, D., Witholt, B. Biocatalyst engineering by assembly of fatty acid transport and oxidation activities for in vivo application of cytochrome P-450BM-3 monooxygenase. Appl Environ Microbiol 1998, 5, 3784
    • (1998) Appl Environ Microbiol , vol.5 , pp. 3784
    • Schneider, S.1    Wubbolts, M.G.2    Sanglard, D.3    Witholt, B.4
  • 8
    • 17444405636 scopus 로고    scopus 로고
    • Biocatalytic production of perillyl alcohol from limonene by using a novel Mycobacterium sp. cytochrome P450 alkane hydroxylase expressed in Pseudomonas putida
    • van Beilen, J.B., Holtackers, R., Luscher, D., Bauer, U., Witholt, B., Duetz, W.A. Biocatalytic production of perillyl alcohol from limonene by using a novel Mycobacterium sp. cytochrome P450 alkane hydroxylase expressed in Pseudomonas putida. Appl Environ Microbiol 2005, 71, 1737.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 1737
    • van Beilen, J.B.1    Holtackers, R.2    Luscher, D.3    Bauer, U.4    Witholt, B.5    Duetz, W.A.6
  • 9
    • 0035037955 scopus 로고    scopus 로고
    • Cost-effective whole-cell assay for laboratory evolution of hydroxylases in Escherichia coli
    • Schwaneberg, U., Otey, C., Cirino, P.C., Farinas, E., Arnold, F.H. Cost-effective whole-cell assay for laboratory evolution of hydroxylases in Escherichia coli. J Biomol Screen 2001, 6, 111.
    • (2001) J Biomol Screen , vol.6 , pp. 111
    • Schwaneberg, U.1    Otey, C.2    Cirino, P.C.3    Farinas, E.4    Arnold, F.H.5
  • 11
    • 31344438135 scopus 로고    scopus 로고
    • Enantioselective epoxidation of terminal alkenes to (R)-and (S)-epoxides by engineered cytochromes P450 BM-3
    • Kubo, T., Peters, M.W., Meinhold, P., Arnold, F.H. Enantioselective epoxidation of terminal alkenes to (R)-and (S)-epoxides by engineered cytochromes P450 BM-3. Chemistry 2006, 12, 1216.
    • (2006) Chemistry , vol.12 , pp. 1216
    • Kubo, T.1    Peters, M.W.2    Meinhold, P.3    Arnold, F.H.4
  • 12
    • 0031473779 scopus 로고    scopus 로고
    • A direct electrode-driven P450 cycle for biocatalysis
    • USA
    • Reipa, V., Mayhew, M.P., Vilker, V.L. A direct electrode-driven P450 cycle for biocatalysis. Proc Natl Acad Sci USA 1997, 94, 13554.
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 13554
    • Reipa, V.1    Mayhew, M.P.2    Vilker, V.L.3
  • 13
    • 0043269709 scopus 로고    scopus 로고
    • A self-suffi cient peroxide-driven hydroxylation biocatalyst
    • Cirino, P.C., Arnold, F.H. A self-suffi cient peroxide-driven hydroxylation biocatalyst. Angew Chem Int Ed 2003, 42, 3299.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 3299
    • Cirino, P.C.1    Arnold, F.H.2
  • 14
    • 0242439281 scopus 로고    scopus 로고
    • Immobilisation of P450 BM-3 and an NADP+ cofactor recycling system: Towards a technical application of hemecontaining monooxygenases in fi ne chemical synthesis
    • Maurer, S.C., Schulze, H., Schmid, R.D., Urlacher, V. Immobilisation of P450 BM-3 and an NADP+ cofactor recycling system: Towards a technical application of hemecontaining monooxygenases in fi ne chemical synthesis. Adv Synth Catal 2003, 345, 802.
    • (2003) Adv Synth Catal , vol.345 , pp. 802
    • Maurer, S.C.1    Schulze, H.2    Schmid, R.D.3    Urlacher, V.4
  • 15
    • 0842278671 scopus 로고    scopus 로고
    • Laboratory evolution of cytochrome p450 BM-3 monooxygenase for organic cosolvents
    • Wong, T.S., Arnold, F.H., Schwaneberg, U. Laboratory evolution of cytochrome p450 BM-3 monooxygenase for organic cosolvents. Biotechnol Bioeng 2004, 85, 351.
    • (2004) Biotechnol Bioeng , vol.85 , pp. 351
    • Wong, T.S.1    Arnold, F.H.2    Schwaneberg, U.3
  • 16
    • 0023654743 scopus 로고
    • Cloning of the gene encoding a catalytically self-suffi cient cytochrome-p-450 fatty-acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts
    • Wen, L.P., Fulco, A.J. Cloning of the gene encoding a catalytically self-suffi cient cytochrome-p-450 fatty-acid monooxygenase induced by barbiturates in Bacillus megaterium and its functional expression and regulation in heterologous (Escherichia coli) and homologous (Bacillus megaterium) hosts. J Biol Chem 1987, 262, 6676.
    • (1987) J Biol Chem , vol.262 , pp. 6676
    • Wen, L.P.1    Fulco, A.J.2
  • 17
    • 0034819837 scopus 로고    scopus 로고
    • Protein engineering of Bacillus megaterium CYP102: The oxidation of polycyclic aromatic hydrocarbons
    • Carmichael, A.B., Wong, L.L. Protein engineering of Bacillus megaterium CYP102: The oxidation of polycyclic aromatic hydrocarbons. Eur J Biochem 2001, 268, 3117.
    • (2001) Eur J Biochem , vol.268 , pp. 3117
    • Carmichael, A.B.1    Wong, L.L.2
  • 18
    • 0011171217 scopus 로고    scopus 로고
    • Regioselectivity and activity of cytochrome P450 BM-3 and mutant F87A in reactions driven by hydrogen peroxide
    • Cirino, P. C., Arnold, F. H. Regioselectivity and activity of cytochrome P450 BM-3 and mutant F87A in reactions driven by hydrogen peroxide. Adv Synth Catal 2002, 344, 932.
    • (2002) Adv Synth Catal , vol.344 , pp. 932
    • Cirino, P.C.1    Arnold, F.H.2
  • 19
    • 0344348884 scopus 로고    scopus 로고
    • A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A
    • Schwaneberg, U., Schmidt-Dannert, C., Schmitt, J., Schmid, R.D. A continuous spectrophotometric assay for P450 BM-3, a fatty acid hydroxylating enzyme, and its mutant F87A. Anal Biochem 1999, 269, 359.
    • (1999) Anal Biochem , vol.269 , pp. 359
    • Schwaneberg, U.1    Schmidt-Dannert, C.2    Schmitt, J.3    Schmid, R.D.4
  • 20
    • 0029809775 scopus 로고    scopus 로고
    • Putidaredoxin reductase-putidaredoxin-cytochrome P450(cam) triple fusion protein-Construction of a self-suffi cient Escherichia coli catalytic system
    • Sibbesen, O., De Voss, J.J., Ortiz De Montellano, P.R. Putidaredoxin reductase-putidaredoxin-cytochrome P450(cam) triple fusion protein-Construction of a self-suffi cient Escherichia coli catalytic system. J Biol Chem 1996, 271, 22462.
    • (1996) J Biol Chem , vol.271 , pp. 22462
    • Sibbesen, O.1    De Voss, J.J.2    Ortiz De Montellano, P.R.3
  • 21
    • 0035661021 scopus 로고    scopus 로고
    • Engineering the CYP101 system for in vivo oxidation of unnatural substrates
    • Bell, S.G., Harford-Cross, C.F., Wong, L.L. Engineering the CYP101 system for in vivo oxidation of unnatural substrates. Protein Eng 2001, 14, 797.
    • (2001) Protein Eng , vol.14 , pp. 797
    • Bell, S.G.1    Harford-Cross, C.F.2    Wong, L.L.3
  • 23
    • 28144461935 scopus 로고    scopus 로고
    • Reconstitution of betacarotene hydroxylase activity of thermostable CYP175A1 monooxygenase
    • Momoi, K., Hofmann, U., Schmid, R.D., Urlacher, V.B. Reconstitution of betacarotene hydroxylase activity of thermostable CYP175A1 monooxygenase. Biochem Biophys Res Commun 2006, 339, 331.
    • (2006) Biochem Biophys Res Commun , vol.339 , pp. 331
    • Momoi, K.1    Hofmann, U.2    Schmid, R.D.3    Urlacher, V.B.4
  • 24
    • 32644461918 scopus 로고    scopus 로고
    • Functional expression system for cytochrome P450 genes using the reductase domain of self-suffi cient P450RhF from Rhodococcus sp.NCIMB 9784
    • Nodate, M., Kubota, M., Misawa, N. Functional expression system for cytochrome P450 genes using the reductase domain of self-suffi cient P450RhF from Rhodococcus sp.NCIMB 9784. Appl Microbiol Biotechnol 2005, 1
    • (2005) Appl Microbiol Biotechnol , pp. 1
    • Nodate, M.1    Kubota, M.2    Misawa, N.3
  • 25
    • 20444375861 scopus 로고    scopus 로고
    • Expanding the alkane oxygenase toolbox: new enzymes and applications
    • Van Beilen, J.B., Funhoff, E.G. Expanding the alkane oxygenase toolbox: new enzymes and applications. Curr Opin Biotechnol 2005, 16, 308.
    • (2005) Curr Opin Biotechnol , vol.16 , pp. 308
    • Van Beilen, J.B.1    Funhoff, E.G.2
  • 27
    • 0023645035 scopus 로고
    • High-resolution crystal structure of cytochrome P450cam
    • Poulos, T.L., Finzel, B.C., Howard, A.J. High-resolution crystal structure of cytochrome P450cam. J Mol Biol 1987, 195, 687.
    • (1987) J Mol Biol , vol.195 , pp. 687
    • Poulos, T.L.1    Finzel, B.C.2    Howard, A.J.3
  • 28
    • 0024208742 scopus 로고
    • The roles of active site hydrogen bonding in cytochrome P450cam as revealed by sitedirected mutagenesis
    • Atkins, W.M., Sligar, S.G. The roles of active site hydrogen bonding in cytochrome P450cam as revealed by sitedirected mutagenesis. J Biol Chem 1988, 263, 18842.
    • (1988) J Biol Chem , vol.263 , pp. 18842
    • Atkins, W.M.1    Sligar, S.G.2
  • 29
    • 0024566973 scopus 로고
    • Molecular recognition in cytochrome P450: alteration of regioselective alkane hydroxylation via protein engineering
    • Atkins, W.M., Sligar, S.G. Molecular recognition in cytochrome P450: alteration of regioselective alkane hydroxylation via protein engineering. J Am Chem Soc 1989, 111, 2715.
    • (1989) J Am Chem Soc , vol.111 , pp. 2715
    • Atkins, W.M.1    Sligar, S.G.2
  • 30
    • 0030749297 scopus 로고    scopus 로고
    • Substrate docking algorithms and prediction of the substrate specifi city of cytochrome P450cam and its L244A mutant
    • De Voss, J.J., Sibbesen, O., Zhang, Z.P., Ortiz de Montellano, P.R. Substrate docking algorithms and prediction of the substrate specifi city of cytochrome P450cam and its L244A mutant. J Am Chem Soc 1997, 119, 5489.
    • (1997) J Am Chem Soc , vol.119 , pp. 5489
    • De Voss, J.J.1    Sibbesen, O.2    Zhang, Z.P.3    Ortiz De Montellano, P.R.4
  • 32
    • 0001385119 scopus 로고
    • The binding and regioselectivity of reaction of (R)-nicotine and (S)-nicotine with cytochrome P-450cam-parallel experimental and theoretical studies
    • Jones, J.P., Trager, W.F., Carlson, T.J. The binding and regioselectivity of reaction of (R)-nicotine and (S)-nicotine with cytochrome P-450cam-parallel experimental and theoretical studies. J Am Chem Soc 1993, 115, 381.
    • (1993) J Am Chem Soc , vol.115 , pp. 381
    • Jones, J.P.1    Trager, W.F.2    Carlson, T.J.3
  • 36
    • 33646806119 scopus 로고    scopus 로고
    • Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium
    • Budde, M., Morr, M., Schmid, R.D., Urlacher, V.B. Selective hydroxylation of highly branched fatty acids and their derivatives by CYP102A1 from Bacillus megaterium. Chembiochem 2006, 7, 789.
    • (2006) Chembiochem , vol.7 , pp. 789
    • Budde, M.1    Morr, M.2    Schmid, R.D.3    Urlacher, V.B.4
  • 38
    • 0031013972 scopus 로고    scopus 로고
    • The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid
    • Li, H., Poulos, T.L. The structure of the cytochrome P450BM-3 haem domain complexed with the fatty acid substrate, palmitoleic acid. Nat Struct Biol 1997, 4, 140.
    • (1997) Nat Struct Biol , vol.4 , pp. 140
    • Li, H.1    Poulos, T.L.2
  • 40
    • 26444481982 scopus 로고    scopus 로고
    • Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy
    • Jovanovic, T., McDermott, A.E. Observation of ligand binding to cytochrome P450 BM-3 by means of solid-state NMR spectroscopy. J Am Chem Soc 2005, 127, 13816.
    • (2005) J Am Chem Soc , vol.127 , pp. 13816
    • Jovanovic, T.1    McDermott, A.E.2
  • 41
    • 33646588326 scopus 로고    scopus 로고
    • Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine, a replica exchange molecular dynamics study
    • Ravindranathan, K.P., Gallicchio, E., Friesner, R.A., McDermott, A.E., Levy, R.M. Conformational equilibrium of cytochrome P450 BM-3 complexed with N-palmitoylglycine, a replica exchange molecular dynamics study. J Am Chem Soc 2006, 128, 5786.
    • (2006) J Am Chem Soc , vol.128 , pp. 5786
    • Ravindranathan, K.P.1    Gallicchio, E.2    Friesner, R.A.3    McDermott, A.E.4    Levy, R.M.5
  • 42
    • 0030660230 scopus 로고    scopus 로고
    • Engineering the substrate specifi city of Bacillus megaterium cytochrome P450 BM3: hydroxylation of alkyl trimethylammonium compounds
    • Oliver, C.F., Modi, S., Primrose, W.U., Lian, L.Y., Roberts, G.C.K. Engineering the substrate specifi city of Bacillus megaterium cytochrome P450 BM3: hydroxylation of alkyl trimethylammonium compounds. Biochem J 1997, 327, 537.
    • (1997) Biochem J , vol.327 , pp. 537
    • Oliver, C.F.1    Modi, S.2    Primrose, W.U.3    Lian, L.Y.4    Roberts, G.C.K.5
  • 45
    • 0035264116 scopus 로고    scopus 로고
    • Structural determinants of active site binding affi nity and metabolism by cytochrome P450 BM-3
    • Cowart, L.A., Falck, J.R., Capdevila, J.H. Structural determinants of active site binding affi nity and metabolism by cytochrome P450 BM-3. Arch Biochem Biophys 2001, 387, 117.
    • (2001) Arch Biochem Biophys , vol.387 , pp. 117
    • Cowart, L.A.1    Falck, J.R.2    Capdevila, J.H.3
  • 46
    • 0031021585 scopus 로고    scopus 로고
    • An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio-and stereoselective (14S,15R)-arachidonic acid epoxygenase
    • Graham-Lorence, S., Truan, G., Peterson, J.A., Falck, J.R., Wei, S., Helvig, C., Capdevila, J.H. An active site substitution, F87V, converts cytochrome P450 BM-3 into a regio-and stereoselective (14S,15R)-arachidonic acid epoxygenase. J Biol Chem 1997, 272, 1127.
    • (1997) J Biol Chem , vol.272 , pp. 1127
    • Graham-Lorence, S.1    Truan, G.2    Peterson, J.A.3    Falck, J.R.4    Wei, S.5    Helvig, C.6    Capdevila, J.H.7
  • 47
    • 0027375275 scopus 로고
    • Molecular recognition in cytochrome P450-mechanism for the control of uncoupling reactions
    • Loida, P.J., Sligar, S.G. Molecular recognition in cytochrome P450-mechanism for the control of uncoupling reactions. Biochemistry 1993, 32, 11530.
    • (1993) Biochemistry , vol.32 , pp. 11530
    • Loida, P.J.1    Sligar, S.G.2
  • 48
    • 0032523238 scopus 로고    scopus 로고
    • Cytochrome P450cam substrate specifi city: Relationship between structure and catalytic oxidation of alkylbenzenes
    • Sibbesen, O., Zhang, Z., Ortiz de Montellano, P.R. Cytochrome P450cam substrate specifi city: Relationship between structure and catalytic oxidation of alkylbenzenes. Arch Biochem Biophys 1998, 353, 285.
    • (1998) Arch Biochem Biophys , vol.353 , pp. 285
    • Sibbesen, O.1    Zhang, Z.2    Ortiz De Montellano, P.R.3
  • 49
    • 0030992065 scopus 로고    scopus 로고
    • The catalytic activity of cytochrome P450cam towards styrene oxidation is increased by sitespecifi c mutagenesis
    • Nickerson, D.P., Harford-Cross, C.F., Fulcher, S.R., Wong, L.L. The catalytic activity of cytochrome P450cam towards styrene oxidation is increased by sitespecifi c mutagenesis. FEBS Lett 1997, 405, 153.
    • (1997) FEBS Lett , vol.405 , pp. 153
    • Nickerson, D.P.1    Harford-Cross, C.F.2    Fulcher, S.R.3    Wong, L.L.4
  • 53
    • 0037227645 scopus 로고    scopus 로고
    • Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy
    • Niaura, G., Reipa, V., Mayhew, M.P., Holden, M., Vilker, V.L. Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy. Arch Biochem Biophys 2003, 409, 102.
    • (2003) Arch Biochem Biophys , vol.409 , pp. 102
    • Niaura, G.1    Reipa, V.2    Mayhew, M.P.3    Holden, M.4    Vilker, V.L.5
  • 54
    • 0031561447 scopus 로고    scopus 로고
    • Selective aliphatic and aromatic carbonhydrogen bond activation catalysed by mutants of cytochrome P450cam
    • Bell, S.G., Rouch, D.A., Wong, L.L. Selective aliphatic and aromatic carbonhydrogen bond activation catalysed by mutants of cytochrome P450cam. J Mol Catal, B Enzym 1997, 3, 293.
    • (1997) J Mol Catal, B Enzym , vol.3 , pp. 293
    • Bell, S.G.1    Rouch, D.A.2    Wong, L.L.3
  • 55
    • 23644456287 scopus 로고    scopus 로고
    • Identifi cation of broad specifi city P450cam variants by primary screening against indole as substrate
    • Celik, A., Speight, R.E., Turner, N.J. Identifi cation of broad specifi city P450cam variants by primary screening against indole as substrate. Chem Commun 2005, 3652.
    • (2005) Chem Commun , pp. 3652
    • Celik, A.1    Speight, R.E.2    Turner, N.J.3
  • 56
    • 0034069318 scopus 로고    scopus 로고
    • Protein engineering of cytochrome P450cam (CYP101) for the oxidation of polycyclic aromatic hydrocarbons
    • Harford-Cross, C.F., Carmichael, A.B., Allan, F.K., England, P.A., Rouch, D.A., Wong, L.-L. Protein engineering of cytochrome P450cam (CYP101) for the oxidation of polycyclic aromatic hydrocarbons. Protein Eng 2000, 13, 121.
    • (2000) Protein Eng , vol.13 , pp. 121
    • Harford-Cross, C.F.1    Carmichael, A.B.2    Allan, F.K.3    England, P.A.4    Rouch, D.A.5    Wong, L.-L.6
  • 57
    • 0034615091 scopus 로고    scopus 로고
    • The oxidation of polychlorinated benzenes by genetically engineered cytochrome P450cam: potential applications in bioremediation
    • Jones, J.P., O'Hare, E.J., Wong, L.L. The oxidation of polychlorinated benzenes by genetically engineered cytochrome P450cam: potential applications in bioremediation. Chem Commun 2000, 247.
    • (2000) Chem Commun , pp. 247
    • Jones, J.P.1    O'Hare, E.J.2    Wong, L.L.3
  • 58
    • 0035081039 scopus 로고    scopus 로고
    • Oxidation of polychlorinated benzenes by genetically engineered CYP101 (cytochrome P450cam)
    • Jones, J.P., O'Hare, E.J., Wong, L.L. Oxidation of polychlorinated benzenes by genetically engineered CYP101 (cytochrome P450cam). Eur J Biochem 2001, 268, 1460.
    • (2001) Eur J Biochem , vol.268 , pp. 1460
    • Jones, J.P.1    O'Hare, E.J.2    Wong, L.L.3
  • 59
    • 0037020229 scopus 로고    scopus 로고
    • Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene
    • Chen, X., Christopher, A., Jones, J.P., Bell, S.G., Guo, Q., Xu, F., Rao, Z., Wong, L.L. Crystal structure of the F87W/Y96F/V247L mutant of cytochrome P-450cam with 1,3,5-trichlorobenzene bound and further protein engineering for the oxidation of pentachlorobenzene and hexachlorobenzene. J Biol Chem 2002, 277, 37519.
    • (2002) J Biol Chem , vol.277 , pp. 37519
    • Chen, X.1    Christopher, A.2    Jones, J.P.3    Bell, S.G.4    Guo, Q.5    Xu, F.6    Rao, Z.7    Wong, L.L.8
  • 60
    • 33644959264 scopus 로고    scopus 로고
    • Conversion of Sphingobium chlorophenolicum ATCC 39723 to a hexachlorobenzene degrader by metabolic engineering
    • Yan, D.Z., Liu, H., Zhou, N.Y. Conversion of Sphingobium chlorophenolicum ATCC 39723 to a hexachlorobenzene degrader by metabolic engineering. Appl Environ Microbiol 2006, 72, 2283.
    • (2006) Appl Environ Microbiol , vol.72 , pp. 2283
    • Yan, D.Z.1    Liu, H.2    Zhou, N.Y.3
  • 61
    • 0035900342 scopus 로고    scopus 로고
    • Residue size at position 87 of cytochrome P450 BM-3 determines its stereoselectivity in propylbenzene and 3-chlorostyrene oxidation
    • Li, Q.S., Ogawa, J., Schmid, R.D., Shimizu, S. Residue size at position 87 of cytochrome P450 BM-3 determines its stereoselectivity in propylbenzene and 3-chlorostyrene oxidation. FEBS Lett 2001, 508, 249.
    • (2001) FEBS Lett , vol.508 , pp. 249
    • Li, Q.S.1    Ogawa, J.2    Schmid, R.D.3    Shimizu, S.4
  • 63
    • 0035653258 scopus 로고    scopus 로고
    • Engineering cytochrome P450 BM-3 for oxidation of polycyclic aromatic hydrocarbons
    • Li, Q.S., Ogawa, J., Schmid, R.D., Shimizu, S. Engineering cytochrome P450 BM-3 for oxidation of polycyclic aromatic hydrocarbons. Appl Environ Microbiol 2001, 67, 5735.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 5735
    • Li, Q.S.1    Ogawa, J.2    Schmid, R.D.3    Shimizu, S.4
  • 65
    • 0035876716 scopus 로고    scopus 로고
    • A P450 BM-3 mutant hydroxylates alkanes, cycloalkanes, arenes and heteroarenes
    • Appel, D., Lutz-Wahl, S., Fischer, P., Schwaneberg, U., Schmid, R.D. A P450 BM-3 mutant hydroxylates alkanes, cycloalkanes, arenes and heteroarenes. J Biotechnol 2001, 88, 167.
    • (2001) J Biotechnol , vol.88 , pp. 167
    • Appel, D.1    Lutz-Wahl, S.2    Fischer, P.3    Schwaneberg, U.4    Schmid, R.D.5
  • 66
    • 0242330792 scopus 로고    scopus 로고
    • Regio-and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3
    • Peters, M.W., Meinhold, P., Glieder, A., Arnold, F.H. Regio-and enantioselective alkane hydroxylation with engineered cytochromes P450 BM-3. J Am Chem Soc 2003, 125, 13442.
    • (2003) J Am Chem Soc , vol.125 , pp. 13442
    • Peters, M.W.1    Meinhold, P.2    Glieder, A.3    Arnold, F.H.4
  • 67
    • 32344437281 scopus 로고    scopus 로고
    • Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system
    • Lentz, O., Feenstra, A., Habicher, T., Hauer, B., Schmid, R.D., Urlacher, V.B. Altering the regioselectivity of cytochrome P450 CYP102A3 of Bacillus subtilis by using a new versatile assay system. Chembiochem 2006, 7, 345.
    • (2006) Chembiochem , vol.7 , pp. 345
    • Lentz, O.1    Feenstra, A.2    Habicher, T.3    Hauer, B.4    Schmid, R.D.5    Urlacher, V.B.6
  • 68
    • 0036842594 scopus 로고    scopus 로고
    • Laboratory evolution of a soluble, selfsuffi cient, highly active alkane hydroxylase
    • Glieder, A., Farinas, E.T., Arnold, F.H. Laboratory evolution of a soluble, selfsuffi cient, highly active alkane hydroxylase. Nat Biotechnol 2002, 20, 1135.
    • (2002) Nat Biotechnol , vol.20 , pp. 1135
    • Glieder, A.1    Farinas, E.T.2    Arnold, F.H.3
  • 69
  • 70
    • 0030464673 scopus 로고    scopus 로고
    • The catalytic oxidation of linear and branched alkanes by cytochrome P450cam
    • Stevenson, J.-A., Westlake, A.C.G., Whittock, C., Wong, L.-L. The catalytic oxidation of linear and branched alkanes by cytochrome P450cam. J Am Chem Soc 1996, 118, 12846.
    • (1996) J Am Chem Soc , vol.118 , pp. 12846
    • Stevenson, J.-A.1    Westlake, A.C.G.2    Whittock, C.3    Wong, L.-L.4
  • 71
    • 0001063177 scopus 로고    scopus 로고
    • Engineering molecular recognition in alkane oxidation catalysed by cytochrome P450cam
    • Stevenson, J.-A., Bearpark, J.K., Wong, L.-L. Engineering molecular recognition in alkane oxidation catalysed by cytochrome P450cam. New J Chem 1998, 551.
    • (1998) New J Chem , pp. 551
    • Stevenson, J.-A.1    Bearpark, J.K.2    Wong, L.-L.3
  • 73
    • 0034739018 scopus 로고    scopus 로고
    • Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site
    • Yoshioka, S., Takahashi, S., Ishimori, K., Morishima, I. Roles of the axial push effect in cytochrome P450cam studied with the site-directed mutagenesis at the heme proximal site. J Inorg Biochem 2000, 81, 141.
    • (2000) J Inorg Biochem , vol.81 , pp. 141
    • Yoshioka, S.1    Takahashi, S.2    Ishimori, K.3    Morishima, I.4
  • 74
    • 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., Poulos, T.L. Crystal structure of the cytochrome p450cam mutant that exhibits the same spectral perturbations induced by putidaredoxin binding. J Biol Chem 2004, 279, 42844.
    • (2004) J Biol Chem , vol.279 , pp. 42844
    • Nagano, S.1    Tosha, T.2    Ishimori, K.3    Morishima, I.4    Poulos, T.L.5
  • 75
    • 21244475208 scopus 로고    scopus 로고
    • The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol
    • Xu, F., Bell, S.G., Lednik, J., Insley, A., Rao, Z., Wong, L.L. The heme monooxygenase cytochrome P450cam can be engineered to oxidize ethane to ethanol. Angew Chem Int Ed 2005, 44, 4029.
    • (2005) Angew Chem Int Ed , vol.44 , pp. 4029
    • Xu, F.1    Bell, S.G.2    Lednik, J.3    Insley, A.4    Rao, Z.5    Wong, L.L.6
  • 76
    • 1542503695 scopus 로고    scopus 로고
    • Engineering the selectivity of aliphatic C-H bond oxidation catalysed by cytochrome P450cam
    • Jones, N.E., England, P.A., Rouch, D.A., Wong, L.L. Engineering the selectivity of aliphatic C-H bond oxidation catalysed by cytochrome P450cam. Chem Commun 1996, 2413.
    • (1996) Chem Commun , pp. 2413
    • Jones, N.E.1    England, P.A.2    Rouch, D.A.3    Wong, L.L.4
  • 78
    • 0031561447 scopus 로고    scopus 로고
    • Selective aliphatic and aromatic carbonhydrogen bond activation catalyzed by mutants of cytochrome P450cam
    • Bell, S.G., Rouch, D.A., Wong, L.-L. Selective aliphatic and aromatic carbonhydrogen bond activation catalyzed by mutants of cytochrome P450cam. J Mol Catal, B Enzym 1997, 3, 293.
    • (1997) J Mol Catal, B Enzym , vol.3 , pp. 293
    • Bell, S.G.1    Rouch, D.A.2    Wong, L.-L.3
  • 80
    • 0037085236 scopus 로고    scopus 로고
    • Active site mutations of cytochrome P450cam alter the binding, coupling, and oxidation of the foreign substrates (R)-and (S)-2-ethylhexanol
    • French, K.J., Rock, D.A., Manchester, J.I., Goldstein, B.M., Jones, J.P. Active site mutations of cytochrome P450cam alter the binding, coupling, and oxidation of the foreign substrates (R)-and (S)-2-ethylhexanol. Arch Biochem Biophys 2002, 398, 188.
    • (2002) Arch Biochem Biophys , vol.398 , pp. 188
    • French, K.J.1    Rock, D.A.2    Manchester, J.I.3    Goldstein, B.M.4    Jones, J.P.5
  • 81
    • 0035859869 scopus 로고    scopus 로고
    • Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies
    • French, K.J., Strickler, M.D., Rock, D.A., Bennett, G.A., Wahlstrom, J.L., Goldstein, B.M., Jones, J.P. Benign synthesis of 2-ethylhexanoic acid by cytochrome P450cam: enzymatic, crystallographic, and theoretical studies. Biochemistry 2001, 40, 9532.
    • (2001) Biochemistry , vol.40 , pp. 9532
    • French, K.J.1    Strickler, M.D.2    Rock, D.A.3    Bennett, G.A.4    Wahlstrom, J.L.5    Goldstein, B.M.6    Jones, J.P.7
  • 82
    • 0035820335 scopus 로고    scopus 로고
    • Engineering the haem monooxygenase cytochrome P450cam for monoterpene oxidation
    • Bell, S.G., Sowden, R.J., Wong, L.-L. Engineering the haem monooxygenase cytochrome P450cam for monoterpene oxidation. Chem Commun 2001, 635.
    • (2001) Chem Commun , pp. 635
    • Bell, S.G.1    Sowden, R.J.2    Wong, L.-L.3
  • 84
    • 11844256914 scopus 로고    scopus 로고
    • Biotransformation of the sesquiterpene (+)-valencene by cytochrome P450cam and P450BM-3
    • Sowden, R.J., Yasmin, S., Rees, N.H., Bell, S.G., Wong, L.L. Biotransformation of the sesquiterpene (+)-valencene by cytochrome P450cam and P450BM-3. Org Biomol Chem 2005, 3, 57.
    • (2005) Org Biomol Chem , vol.3 , pp. 57
    • Sowden, R.J.1    Yasmin, S.2    Rees, N.H.3    Bell, S.G.4    Wong, L.L.5
  • 88
    • 32544436092 scopus 로고    scopus 로고
    • Preparation of human metabolites of propranolol using laboratory-evolved bacterial cytochromes P450
    • Otey, C.R., Bandara, G., Lalonde, J., Takahashi, K., Arnold, F.H. Preparation of human metabolites of propranolol using laboratory-evolved bacterial cytochromes P450. Biotechnol. Bioeng 2006, 93, 494.
    • (2006) Biotechnol. Bioeng , vol.93 , pp. 494
    • Otey, C.R.1    Bandara, G.2    Lalonde, J.3    Takahashi, K.4    Arnold, F.H.5
  • 89
    • 33646505950 scopus 로고    scopus 로고
    • Enantioselective alpha-hydroxylation of 2-arylacetic acid derivatives and buspirone catalyzed by engineered cytochrome P450 BM-3
    • Landwehr, M., Hochrein, L., Otey, C.R., Kasrayan, A., Backvall, J.E., Arnold, F.H. Enantioselective alpha-hydroxylation of 2-arylacetic acid derivatives and buspirone catalyzed by engineered cytochrome P450 BM-3. J Am Chem Soc 2006, 128, 6058.
    • (2006) J Am Chem Soc , vol.128 , pp. 6058
    • Landwehr, M.1    Hochrein, L.2    Otey, C.R.3    Kasrayan, A.4    Backvall, J.E.5    Arnold, F.H.6
  • 90
    • 33745652737 scopus 로고    scopus 로고
    • Cytochrome P450 monooxygenases: perspectives for synthetic application
    • Urlacher, V.B., Eiben, S. Cytochrome P450 monooxygenases: perspectives for synthetic application. Trends Biotechnol 2006, 24, 324.
    • (2006) Trends Biotechnol , vol.24 , pp. 324
    • Urlacher, V.B.1    Eiben, S.2
  • 91
    • 33645244308 scopus 로고    scopus 로고
    • Recent advances in oxygenase-catalyzed biotransformations
    • Urlacher, V.B., Schmid, R.D. Recent advances in oxygenase-catalyzed biotransformations. Curr Opin Chem Biol 2006, 10, 156.
    • (2006) Curr Opin Chem Biol , vol.10 , pp. 156
    • Urlacher, V.B.1    Schmid, R.D.2


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