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Volumn 49, Issue 8, 2010, Pages 1678-1688

Structure and ligand binding properties of the epoxidase component of styrene monooxygenase

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BINDING EQUILIBRIA; COOPERATIVE INTERACTIONS; HOMODIMERS; ISOTHERMAL TITRATION CALORIMETRY; LIGAND BINDING PROPERTIES; MONOOXYGENASES; OXYGEN REACTION; P-HYDROXYBENZOATE HYDROXYLASE; REACTION ORDERS; REDOX EQUILIBRIUM; RESTING STATE; SECONDARY STRUCTURES; STRUCTURAL COMPARISON; STYRENE OXIDE; TIGHTLY-COUPLED; TWO-COMPONENT;

EID: 77749252741     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi901693u     Document Type: Article
Times cited : (61)

References (50)
  • 1
    • 27544432463 scopus 로고    scopus 로고
    • Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases
    • DOI 10.1016/j.bbrc.2005.09.081, PII S0006291X0502108X
    • Ballou, D. P., Entsch, B., and Cole, L. J. (2005) Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases. Biochem. Biophys. Res. Commun. 338, 590-598. (Pubitemid 41540607)
    • (2005) Biochemical and Biophysical Research Communications , vol.338 , Issue.1 , pp. 590-598
    • Ballou, D.P.1    Entsch, B.2    Cole, L.J.3
  • 2
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • van Berkel, W. J. H., Kamerbeek, N. M., and Fraaije, M. W. (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts. J. Biotechnol. 124, 670-689.
    • (2006) J. Biotechnol. , vol.124 , pp. 670-689
    • Van Berkel, W.J.H.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 3
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins. J.Biol. Chem. 269, 22459-22462.
    • (1994) J.Biol. Chem. , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 5
    • 0029001789 scopus 로고
    • Flavoprotein structure and mechanism. 1. Structure and mechanism of para-hydroxybenzoate hydroxylase
    • Entsch, B., and Vanberkel, W. J. H. (1995) Flavoprotein structure and mechanism. 1. Structure and mechanism of para-hydroxybenzoate hydroxylase. FASEB J. 9, 476-483.
    • (1995) FASEB J , vol.9 , pp. 476-483
    • Entsch, B.1    Vanberkel, W.J.H.2
  • 6
    • 0032524753 scopus 로고    scopus 로고
    • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
    • Enroth,C.,Neujahr,H.,Schneider,G.,andLindqvist,Y.(1998) Thecrystalstructureofphenolhydroxylaseincomplexwith FADandphenolprovidesevidenceforaconcertedconformationalchangeintheen zymeanditscofactorduringcatalysis.Structure6,605-617.(Pubitemid28258113)
    • (1998) Structure , vol.6 , Issue.5 , pp. 605-617
    • Enroth, C.1    Neujahr, H.2    Schneider, G.3    Lindqvist, Y.4
  • 7
    • 0035900019 scopus 로고    scopus 로고
    • Studies of the mechanism of phenol hydroxylase: Mutants Tyr289Phe, Asp54Asn, and Arg281Met
    • DOI 10.1021/bi010962y
    • Xu, D., Ballou, D. P., and Massey, V. (2001) Studies of the mechanism of phenol hydroxylase: Mutants Tyr289Phe, Asp54Asn, and Arg281-Met. Biochemistry 40, 12369-12378. (Pubitemid 32959759)
    • (2001) Biochemistry , vol.40 , Issue.41 , pp. 12369-12378
    • Xu, D.1    Ballou, D.P.2    Massey, V.3
  • 9
    • 0034652257 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase
    • DOI 10.1006/abbi.1999.1629
    • Laden, B. P., Tang, Y., and Porter, T. D. (2000) Cloning, heterologous expression, and enzymological characterization of human squalene monooxygenase. Arch. Biochem. Biophys. 374, 381-388. (Pubitemid 30120276)
    • (2000) Archives of Biochemistry and Biophysics , vol.374 , Issue.2 , pp. 381-388
    • Laden, B.P.1    Tang, Y.2    Porter, T.D.3
  • 11
    • 0025253582 scopus 로고
    • Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase
    • Hartmans,S.,vanderWerf,M.J.,anddeBont,J.A.(1990) Bacterialdegradationofstyreneinvolvinganovelflavinadeninedinucleotide dependentstyrenemonooxygenase.Anal.Environ.Microbiol.56,1347-1351. (Pubitemid20147211)
    • (1990) Applied and Environmental Microbiology , vol.56 , Issue.5 , pp. 1347-1351
    • Hartmans, S.1    Van Der Werf, M.J.2    De Bont, J.A.3
  • 12
    • 0031745849 scopus 로고    scopus 로고
    • Towards a biocatalyst for (S)-styrene oxide production: Characterization of the styrene degradation pathway of Pseudomonas sp. strain VLB120
    • Panke,S.,Witholt,B.,Schmid,A.,andWubbolts,M.G.(1998) Towardsabiocatalystfor(S)-styreneoxideproduction: CharacterizationofthestyrenedegradationpathwayofPseudomonassstrainVLB120.Appl. Environ.Microbiol.64,2032-2043.(Pubitemid28252761)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.6 , pp. 2032-2043
    • Panke, S.1    Witholt, B.2    Schmid, A.3    Wubbolts, M.G.4
  • 13
    • 0038344024 scopus 로고    scopus 로고
    • Stereospecific biocatalytic epoxidation: The first example of direct regeneration of a FAD-dependent monooxygenase for catalysis
    • DOI 10.1021/ja034119u
    • Hollmann, F., Lin, P. C., Witholt, B., and Schmid, A. (2003) Stereospecific biocatalytic epoxidation: The first example of direct regeneration of a FAD-dependent monooxygenase for catalysis. J. Am. Chem. Soc. 125, 8209-8217. (Pubitemid 36828584)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.27 , pp. 8209-8217
    • Hollmann, F.1    Lin, P.-C.2    Witholt, B.3    Schmid, A.4
  • 14
    • 3843128465 scopus 로고    scopus 로고
    • Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase
    • DOI 10.1128/JB.186.16.5292-5302.2004
    • Otto, K., Hofstetter, K., Rothlisberger, M., Witholt, B., and Schmid, A. (2004) Biochemical characterization of StyAB from Pseudomonas sp. strain VLBl20 as a two-component flavin-diffusible monooxygenase. J. Bacteriol. 186, 5292-5302. (Pubitemid 39043671)
    • (2004) Journal of Bacteriology , vol.186 , Issue.16 , pp. 5292-5302
    • Otto, K.1    Hofstetter, K.2    Rothlisberger, M.3    Witholt, B.4    Schmid, A.5
  • 15
    • 24944534515 scopus 로고    scopus 로고
    • Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase
    • DOI 10.1016/j.abb.2005.07.020, PII S0003986105003061
    • Kantz, A., Chin, F., Nallamothu, N., Nguyen, T., and Gassner, G. T. (2005) Mechanism of flavin transfer and oxygen activation by the twocomponent flavoenzyme styrene monooxygenase. Arch. Biochem. Biophys. 442, 102-116. (Pubitemid 41330996)
    • (2005) Archives of Biochemistry and Biophysics , vol.442 , Issue.1 , pp. 102-116
    • Kantz, A.1    Chin, F.2    Nallamothu, N.3    Nguyen, T.4    Gassner, G.T.5
  • 16
    • 0034609021 scopus 로고    scopus 로고
    • Production of enantiopure styrene oxide by recombinant Escherichia coli synthesizing a two-component styrene monooxygenase
    • DOI 10.1002/(SICI)1097-0290(20000705)69:1<91::AID-BIT11>3.0.CO;2-X
    • Panke, S., Wubbolts, M. G., Schmid, A., and Witholt, B. (2000) Production of enantiopure styrene oxide by recombinant Escherichia coli synthesizing a two-component styrene monooxygenase. Bioteehnol. Bioeng. 69, 91-100. (Pubitemid 30418266)
    • (2000) Biotechnology and Bioengineering , vol.69 , Issue.1 , pp. 91-100
    • Panke, S.1    Wubbolts, M.G.2    Schmid, A.3    Witholt, B.4
  • 17
    • 0000499563 scopus 로고    scopus 로고
    • Integrated biocatalytic synthesis on gram scale: The highly enantioselective preparation of chiral oxiranes with styrene monooxygenase
    • Schmid,A.,Hofstetter,K.,Feiten,H.J.,Hollmann,F.,andWitholt,B.(2001) Integratedbiocatalyticsynthesisongramscale: Thehighlyenantioselectivepreparationofchiraloxiraneswithstyrenemonooxygenase. Adv.Synth.Catal.343,732-737.(Pubitemid33679791)
    • (2001) Advanced Synthesis and Catalysis , vol.343 , Issue.6-7 , pp. 732-737
    • Schmid, A.1    Hofstetter, K.2    Feiten, H.-J.3    Hollmann, F.4    Witholt, B.5
  • 18
    • 0346736498 scopus 로고    scopus 로고
    • Complex formation between Vibrio harveyi luciferase and monomeric NADPH: FMN oxidoreductase
    • Jeffers, C. E., Nichols, J. C., and Tu, S. C. (2003) Complex formation between Vibrio harveyi luciferase and monomeric NADPH: FMN oxidoreductase. Biochemistry 42, 529-534.
    • (2003) Biochemistry , vol.42 , pp. 529-534
    • Jeffers, C.E.1    Nichols, J.C.2    Tu, S.C.3
  • 19
    • 33751560654 scopus 로고    scopus 로고
    • Detection of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli
    • DOI 10.1128/JB.00966-06
    • Abdurachim, K., and Ellis, H. R. (2006) Detection, of protein-protein interactions in the alkanesulfonate monooxygenase system from Escherichia coli. Bacteriol. 188, 8153-8159. (Pubitemid 44845686)
    • (2006) Journal of Bacteriology , vol.188 , Issue.23 , pp. 8153-8159
    • Abdurachim, K.1    Ellis, H.R.2
  • 20
    • 70450228475 scopus 로고    scopus 로고
    • Two lysine residues in the bacterial luciferase mobile loop stabilize reaction intermediates
    • Campbell, Z. T., and Baldwin, T. O. (2009) Two lysine residues in the bacterial luciferase mobile loop stabilize reaction intermediates. J. Biol. Chem. 284, 32827-32834.
    • (2009) J. Biol. Chem. , vol.284 , pp. 32827-32834
    • Campbell, Z.T.1    Baldwin, T.O.2
  • 21
    • 34547095238 scopus 로고    scopus 로고
    • Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase
    • Sucharitakul, J., Phongsak, T., Entsch, B., Svasti, J., Chaiyen, P., and Bailou, D. P. (2007) Kinetics of a two-component p-hydroxyphenylacetate hydroxylase explain how reduced flavin is transferred from the reductase to the oxygenase. Biochemistry 46, 8611-8623.
    • (2007) Biochemistry , vol.46 , pp. 8611-8623
    • Sucharitakul, J.1    Phongsak, T.2    Entsch, B.3    Svasti, J.4    Chaiyen, P.5    Bailou, D.P.6
  • 22
    • 0342514774 scopus 로고    scopus 로고
    • Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: A prototype of a new Flavin:NAD(P)H reductase subfamily
    • Galan, B., Diaz, E., Prieto, M. A., and Garcia, J. L. (2000) Functional analysis of the small component of the 4-hydroxyphenylacetate 3-monooxygenase of Escherichia coli W: A prototype of a new Flavin:NAD(P)H reductase subfamily. J. Bacteriol. 182, 627-636.
    • (2000) J. Bacteriol. , vol.182 , pp. 627-636
    • Galan, B.1    Diaz, E.2    Prieto, M.A.3    Garcia, J.L.4
  • 23
    • 0038746745 scopus 로고    scopus 로고
    • 2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase
    • 2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. Biochemistry 42, 7509-7517.
    • (2003) Biochemistry , vol.42 , pp. 7509-7517
    • Louie, T.M.1    Xie, X.S.2    Xun, L.3
  • 24
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinoski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 26
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • DOI 10.1016/S0076-6879(97)76073-7
    • de la Forteile, E., and Bricogne, G. (1997) Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Emzymol. 276, 472-494. (Pubitemid 27085618)
    • (1997) Methods in Enzymology , vol.276 , pp. 472-494
    • De La Forteile, E.1    Bricogne, G.2
  • 27
    • 0036793095 scopus 로고    scopus 로고
    • Substructure solution with SHELXD
    • Schneider, T. R., and Sheldrick, G. M. (2002) Substructure solution with SHELXD. Aga Crystallogr. D58, 1772-1779.
    • (2002) Aga Crystallogr. , vol.D58 , pp. 1772-1779
    • Schneider, T.R.1    Sheldrick, G.M.2
  • 29
    • 33748337934 scopus 로고    scopus 로고
    • The Buccaneer software for automated model building. 1. Tracing protein chains
    • Cowtan, K. (2006) The Buccaneer software for automated model building. 1. Tracing protein chains, Acta Crystallogr. D62, 1002-1011.
    • (2006) Acta Crystallogr , vol.D62 , pp. 1002-1011
    • Cowtan, K.1
  • 31
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. D53, 240-255.
    • (1997) Acta Crystallogr. , vol.D53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A. (1993) PROCHECK: A program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1
  • 35
    • 0028103275 scopus 로고
    • The CCP4 suite programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite programs for protein crystallography, Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 36
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissnel, E., and Henrick, K. (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr. D60, 2256-2268.
    • (2004) Acta Crystallogr. , vol.D60 , pp. 2256-2268
    • Krissnel, E.1    Henrick, K.2
  • 37
    • 33747818007 scopus 로고    scopus 로고
    • CASTp: Computed atlas of surface topography of proteins with structural and topographical mapping of functionally annotated residues
    • DOI 10.1093/nar/gkl282
    • Dundas, J., Ouyang, Z., Tseng, J., Binkowski, A., Turpaz, Y., and Liang, J. (2006) CASTp: Computed atlas of surface topograhy of proteins with structural and topographical mapping of functionally annotated residues, Nucleic Acids Res. 34, W116-W118. (Pubitemid 44529746)
    • (2006) Nucleic Acids Research , vol.34 , Issue.WEB. SERV. ISS
    • Dundas, J.1    Ouyang, Z.2    Tseng, J.3    Binkowski, A.4    Turpaz, Y.5    Liang, J.6
  • 38
    • 65349114255 scopus 로고    scopus 로고
    • ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments
    • Bond, C. S., and Schüttelkopf, W. (2009) ALINE: A WYSIWYG protein-sequence alignment editor for publication-quality alignments, Acta Crystallogr. D65, 510-512.
    • (2009) Acta Crystallogr. , vol.D65 , pp. 510-512
    • Bond, C.S.1    Schüttelkopf, W.2
  • 39
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with daliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm, L., Kaariainen, S., Rosenstrom, P., and Schenkel, A. (2008) Searching protein structure databases with DaliLite v.3. Bioinformgtics24, 2780-2781. (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 41
    • 36348950818 scopus 로고    scopus 로고
    • Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8
    • DOI 10.1074/jbc.M703440200
    • Kim, S. H., Hisano, T., Takeda, K., Iwasaki, W., Ebihara, A., and Miki, K. (2007) Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from. Thermus thermophilus HB8. J. Biol. Chem. 282, 33107-33117. (Pubitemid 350159282)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.45 , pp. 33107-33117
    • Kim, S.-H.1    Hisano, T.2    Takeda, K.3    Iwasaki, W.4    Ebihara, A.5    Miki, K.6
  • 42
    • 0032588643 scopus 로고    scopus 로고
    • Phel61 and Argl66 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability
    • Eppink, M. H., Bunthol, C., Schreuder, H. A., and van Berkel, W. J. (1999) Phel61 and Argl66 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability. FEBS Lett. 443, 251-255.
    • (1999) FEBS Lett , vol.443 , pp. 251-255
    • Eppink, M.H.1    Bunthol, C.2    Schreuder, H.A.3    Van Berkel, W.J.4
  • 45
    • 0024974962 scopus 로고
    • Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution. Analysis of the enzyme-substrate and enzyme-product complexes
    • Schreuder, H. A., Prick, P. A., Wierenga, R. K., Vriend, G., Wilson, K. S., Hol, W. G., and Drenth, J. (1989) Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 Å resolution. Analysis of the enzyme-substrate and enzyme-product complexes. J. Mol. Biol. 208, 679-696.
    • (1989) J. Mol. Biol. , vol.208 , pp. 679-696
    • Schreuder, H.A.1    Prick, P.A.2    Wierenga, R.K.3    Vriend, G.4    Wilson, K.S.5    Hol, W.G.6    Drenth, J.7
  • 46
    • 33751105570 scopus 로고    scopus 로고
    • Crystal Structure of 3-Hydroxybenzoate Hydroxylase from Comamonas testosteroni Has a Large Tunnel for Substrate and Oxygen Access to the Active Site
    • DOI 10.1016/j.jmb.2006.09.031, PII S0022283606012228
    • Hiromoto, T., Fujiwara, S., Hosokawa, K., and Yamaguchi, H. (2006) Crystal structure of 3-hydroxybenzoate hydroxylase from Comamonas testosteroni has a large tunnel for substrate and oxygen access to the active site. J. Mol. Biol. 364, 878-896. (Pubitemid 44765035)
    • (2006) Journal of Molecular Biology , vol.364 , Issue.5 , pp. 878-896
    • Hiromoto, T.1    Fujiwara, S.2    Hosokawa, K.3    Yamaguchi, H.4
  • 47
    • 33751231122 scopus 로고    scopus 로고
    • Enantioselective substrate binding in a monooxygenase protein model by molecular dynamics and docking
    • DOI 10.1529/biophysj.106.088633
    • Feenstra, K. A., Hofstetter, K., Bosch, R., Schmid, A., Commandeur, J. N., and Vermeulen, N. P. (2006) Enantioselective substrate binding in a monooxygenase protein model by molecular dynamics and docking. Biophys. J. 91, 3206-3216. (Pubitemid 44788255)
    • (2006) Biophysical Journal , vol.91 , Issue.9 , pp. 3206-3216
    • Feenstra, K.A.1    Hofstetter, K.2    Bosch, R.3    Schmid, A.4    Commandeur, J.N.5    Vermeulen, N.P.6
  • 48
    • 9744270010 scopus 로고    scopus 로고
    • Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase
    • DOI 10.1016/j.abb.2004.09.029, PII S0003986104005454
    • Entsch, B., Cole, L. J., and Bailou, D. P. (2005) Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase. Arch. Biochem. Biophys. 433, 297-311. (Pubitemid 39586600)
    • (2005) Archives of Biochemistry and Biophysics , vol.433 , Issue.1 , pp. 297-311
    • Entsch, B.1    Cole, L.J.2    Ballou, D.P.3
  • 49
    • 0035799327 scopus 로고    scopus 로고
    • Protein dynamics control proton, transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase
    • Frederick, K. K., Bailou, D. P., and Palfey, B. A. (2001) Protein dynamics control proton, transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase. Biochemistry 40, 3891-3899.
    • (2001) Biochemistry , vol.40 , pp. 3891-3899
    • Frederick, K.K.1    Bailou, D.P.2    Palfey, B.A.3


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