메뉴 건너뛰기




Volumn 52, Issue 35, 2013, Pages 6063-6075

Structure and mechanism of styrene monooxygenase reductase: New insight into the FAD-transfer reaction

Author keywords

[No Author keywords available]

Indexed keywords

COMPETITIVE REDUCTION; ELECTRON-TRANSFER REACTIONS; HYDRIDE-TRANSFER REACTION; PEROXIDE INTERMEDIATE; PROTEIN-PROTEIN INTERACTIONS; PSEUDOMONAS PUTIDA; PYRIDINE NUCLEOTIDES; STYRENE MONOOXYGENASE;

EID: 84883475914     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400763h     Document Type: Article
Times cited : (42)

References (40)
  • 1
    • 77956631904 scopus 로고    scopus 로고
    • Removal of saturated aliphatic hydrocarbons (gasoline components) from air via bacterial biofiltration
    • Paca, J., Halecky, M., Vanek, T., Kozliak, E., and Jones, K. (2010) Removal of saturated aliphatic hydrocarbons (gasoline components) from air via bacterial biofiltration J. Environ. Sci. Health, Part A 45, 1037-1047
    • (2010) J. Environ. Sci. Health, Part A , vol.45 , pp. 1037-1047
    • Paca, J.1    Halecky, M.2    Vanek, T.3    Kozliak, E.4    Jones, K.5
  • 2
    • 34249097403 scopus 로고    scopus 로고
    • Metabolism of phenylalanine and biosynthesis of styrene in Penicillium camemberti
    • Pagot, Y., Belin, J. M., Husson, F., and Spinnler, H. E. (2007) Metabolism of phenylalanine and biosynthesis of styrene in Penicillium camemberti J. Dairy Res. 74, 180-185
    • (2007) J. Dairy Res. , vol.74 , pp. 180-185
    • Pagot, Y.1    Belin, J.M.2    Husson, F.3    Spinnler, H.E.4
  • 3
    • 33947101113 scopus 로고    scopus 로고
    • Butadiene production process overview
    • White, W. C. (2007) Butadiene production process overview Chem.-Biol. Interact. 166, 10-14
    • (2007) Chem.-Biol. Interact. , vol.166 , pp. 10-14
    • White, W.C.1
  • 5
    • 0036643392 scopus 로고    scopus 로고
    • Degradation of polystyrene using clinoptilolite catalysts
    • Lee, S., Yoon, J., Kim, J., and Park, D. (2002) Degradation of polystyrene using clinoptilolite catalysts J. Anal. Appl. Pyrolysis 64, 71-83
    • (2002) J. Anal. Appl. Pyrolysis , vol.64 , pp. 71-83
    • Lee, S.1    Yoon, J.2    Kim, J.3    Park, D.4
  • 8
    • 35848961221 scopus 로고    scopus 로고
    • Synthesis and characterization of styrene oxide adducts with cysteine, histidine, and lysine in human globin
    • Jagr, M., Mraz, J., Linhart, I., Stransky, V., and Pospisil, M. (2007) Synthesis and characterization of styrene oxide adducts with cysteine, histidine, and lysine in human globin Chem. Res. Toxicol. 20, 1442-1452
    • (2007) Chem. Res. Toxicol. , vol.20 , pp. 1442-1452
    • Jagr, M.1    Mraz, J.2    Linhart, I.3    Stransky, V.4    Pospisil, M.5
  • 9
    • 0034214007 scopus 로고    scopus 로고
    • Styrene oxide-induced 2′-deoxycytidine adducts: Implications for the mutagenicity of styrene oxide
    • Koskinen, M., Calebiro, D., and Hemminki, K. (2000) Styrene oxide-induced 2′-deoxycytidine adducts: Implications for the mutagenicity of styrene oxide Chem.-Biol. Interact. 126, 201-213
    • (2000) Chem.-Biol. Interact. , vol.126 , pp. 201-213
    • Koskinen, M.1    Calebiro, D.2    Hemminki, K.3
  • 10
    • 1642471677 scopus 로고    scopus 로고
    • Metabolism and toxicity of the styrene metabolite 4-vinylphenol in CYP2E1 knockout mice
    • Vogie, K., Mantick, N., and Carlson, G. (2004) Metabolism and toxicity of the styrene metabolite 4-vinylphenol in CYP2E1 knockout mice J. Toxicol. Environ. Health, Part A 67, 145-152
    • (2004) J. Toxicol. Environ. Health, Part A , vol.67 , pp. 145-152
    • Vogie, K.1    Mantick, N.2    Carlson, G.3
  • 12
    • 0025253582 scopus 로고
    • Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase
    • Hartmans, S., van der Werf, M. J., and de Bont, J. A. (1990) Bacterial degradation of styrene involving a novel flavin adenine dinucleotide-dependent styrene monooxygenase Appl. Environ. Microbiol. 56, 1347-1351
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1347-1351
    • Hartmans, S.1    Van Der Werf, M.J.2    De Bont, J.A.3
  • 13
    • 0029971779 scopus 로고    scopus 로고
    • Styrene metabolism in Exophiala jeanselmei and involvement of a cytochrome P-450-dependent styrene monooxygenase
    • Cox, H. H., Faber, B. W., Van Heiningen, W. N., Radhoe, H., Doddema, H. J., and Harder, W. (1996) Styrene metabolism in Exophiala jeanselmei and involvement of a cytochrome P-450-dependent styrene monooxygenase Appl. Environ. Microbiol. 62, 1471-1474
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1471-1474
    • Cox, H.H.1    Faber, B.W.2    Van Heiningen, W.N.3    Radhoe, H.4    Doddema, H.J.5    Harder, W.6
  • 14
  • 15
    • 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
  • 16
    • 80052794668 scopus 로고    scopus 로고
    • Catalytic and structural features of flavoprotein hydroxylases and epoxidases
    • Montersino, S., Tischler, D., Gassner, G. T., and van Berkel, W. J. H. (2011) Catalytic and structural features of flavoprotein hydroxylases and epoxidases Adv. Synth. Catal. 353, 2301-2319
    • (2011) Adv. Synth. Catal. , vol.353 , pp. 2301-2319
    • Montersino, S.1    Tischler, D.2    Gassner, G.T.3    Van Berkel, W.J.H.4
  • 17
    • 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
  • 18
    • 77952545697 scopus 로고    scopus 로고
    • The FMN-dependent two-component monooxygenase systems
    • Ellis, H. R. (2011) The FMN-dependent two-component monooxygenase systems Arch. Biochem. Biophys. 497, 1-12
    • (2011) Arch. Biochem. Biophys. , vol.497 , pp. 1-12
    • Ellis, H.R.1
  • 19
    • 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 Ballou, 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    Ballou, D.P.6
  • 20
    • 44849143455 scopus 로고    scopus 로고
    • Mechanism and regulation of the two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor
    • Valton, J., Mathevon, C., Fontecave, M., Nivière, V., and Ballou, D. P. (2008) Mechanism and regulation of the two-component FMN-dependent monooxygenase ActVA-ActVB from Streptomyces coelicolor J. Biol. Chem. 283, 10287-10296
    • (2008) J. Biol. Chem. , vol.283 , pp. 10287-10296
    • Valton, J.1    Mathevon, C.2    Fontecave, M.3    Nivieìre, V.4    Ballou, D.P.5
  • 21
    • 7244236628 scopus 로고    scopus 로고
    • A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor
    • Valton, J., Filisetti, L., Fontecave, M., and Nivière, V. (2004) A two-component flavin-dependent monooxygenase involved in actinorhodin biosynthesis in Streptomyces coelicolor J. Biol. Chem. 279, 44362-44369
    • (2004) J. Biol. Chem. , vol.279 , pp. 44362-44369
    • Valton, J.1    Filisetti, L.2    Fontecave, M.3    Nivieìre, V.4
  • 22
    • 79952092735 scopus 로고    scopus 로고
    • Nature of the reaction intermediates in the flavin adenine dinucleotide-dependent epoxidation mechanism of styrene monooxygenase
    • Kantz, A. and Gassner, G. T. (2011) Nature of the reaction intermediates in the flavin adenine dinucleotide-dependent epoxidation mechanism of styrene monooxygenase Biochemistry 50, 523-532
    • (2011) Biochemistry , vol.50 , pp. 523-532
    • Kantz, A.1    Gassner, G.T.2
  • 23
    • 77749252741 scopus 로고    scopus 로고
    • Structure and ligand binding properties of the epoxidase component of styrene monooxygenase
    • Ukaegbu, U. E., Kantz, A., Beaton, M., Gassner, G. T., and Rosenzweig, A. C. (2010) Structure and ligand binding properties of the epoxidase component of styrene monooxygenase Biochemistry 49, 1678-1688
    • (2010) Biochemistry , vol.49 , pp. 1678-1688
    • Ukaegbu, U.E.1    Kantz, A.2    Beaton, M.3    Gassner, G.T.4    Rosenzweig, A.C.5
  • 24
    • 3843128465 scopus 로고    scopus 로고
    • Biochemical characterization of StyAB from Pseudomonas sp. Strain VLB120 as a two-component flavin-diffusible monooxygenase
    • Otto, K., Hofstetter, K., Rothlisberger, M., Witholt, B., and Schmid, A. (2004) Biochemical characterization of StyAB from Pseudomonas sp. strain VLB120 as a two-component flavin-diffusible monooxygenase J. Bacteriol. 186, 5292-5302
    • (2004) J. Bacteriol. , vol.186 , pp. 5292-5302
    • Otto, K.1    Hofstetter, K.2    Rothlisberger, M.3    Witholt, B.4    Schmid, A.5
  • 25
    • 0038746745 scopus 로고    scopus 로고
    • Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase
    • Louie, T. M., Xie, X. S., and Xun, L. (2003) Coordinated production and utilization of FADH2 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
  • 26
    • 24944534515 scopus 로고    scopus 로고
    • Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase
    • Kantz, A., Chin, F., Nallamothu, N., Nguyen, T., and Gassner, G. T. (2005) Mechanism of flavin transfer and oxygen activation by the two-component flavoenzyme styrene monooxygenase Arch. Biochem. Biophys. 442, 102-116
    • (2005) Arch. Biochem. Biophys. , vol.442 , pp. 102-116
    • Kantz, A.1    Chin, F.2    Nallamothu, N.3    Nguyen, T.4    Gassner, G.T.5
  • 27
    • 0038344024 scopus 로고    scopus 로고
    • Stereospecific biocatalytic epoxidation: The first example of direct regeneration of a FAD-dependent monooxygenase for catalysis
    • 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
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 8209-8217
    • Hollmann, F.1    Lin, P.-C.2    Witholt, B.3    Schmid, A.4
  • 28
    • 18644384980 scopus 로고    scopus 로고
    • Direct electrochemical regeneration of monooxygenase subunits for biocatalytic asymmetric epoxidation
    • Hollmann, F., Hofstetter, K., Habicher, T., Hauer, B., and Schmid, A. (2005) Direct electrochemical regeneration of monooxygenase subunits for biocatalytic asymmetric epoxidation J. Am. Chem. Soc. 127, 6540-6541
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 6540-6541
    • Hollmann, F.1    Hofstetter, K.2    Habicher, T.3    Hauer, B.4    Schmid, A.5
  • 29
    • 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
  • 30
    • 1842424838 scopus 로고    scopus 로고
    • Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action
    • van den Heuvel, R. H., Westphal, A. H., Heck, A. J., Walsh, M. A., Rovida, S., van Berkel, W. J., and Mattevi, A. (2004) Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action J. Biol. Chem. 279, 12860-12867
    • (2004) J. Biol. Chem. , vol.279 , pp. 12860-12867
    • Van Den Heuvel, R.H.1    Westphal, A.H.2    Heck, A.J.3    Walsh, M.A.4    Rovida, S.5    Van Berkel, W.J.6    Mattevi, A.7
  • 31
    • 38549124488 scopus 로고    scopus 로고
    • Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity
    • Kim, S.-H., Hisano, T., Iwasaki, W., Ebihara, A., and Miki, K. (2007) Crystal structure of the flavin reductase component (HpaC) of 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8: Structural basis for the flavin affinity Proteins 70, 718-730
    • (2007) Proteins , vol.70 , pp. 718-730
    • Kim, S.-H.1    Hisano, T.2    Iwasaki, W.3    Ebihara, A.4    Miki, K.5
  • 32
    • 0019887896 scopus 로고
    • Steroidogenic electron transport by adrenodoxin reductase and adrenodoxin. Use of acetylated cytochrome c as a mechanistic probe of electron transfer
    • Lambeth, J. D., Lancaster, J. R., and Kamin, H. (1981) Steroidogenic electron transport by adrenodoxin reductase and adrenodoxin. Use of acetylated cytochrome c as a mechanistic probe of electron transfer J. Biol. Chem. 256, 3674-3678
    • (1981) J. Biol. Chem. , vol.256 , pp. 3674-3678
    • Lambeth, J.D.1    Lancaster, J.R.2    Kamin, H.3
  • 33
    • 0019883890 scopus 로고
    • Stabilization of the red semiquinone form of pig kidney general acyl-CoA dehydrogenase by acyl coenzyme A derivatives
    • Mizzer, J. P. and Thorpe, C. (1981) Stabilization of the red semiquinone form of pig kidney general acyl-CoA dehydrogenase by acyl coenzyme A derivatives Biochemistry 20, 4965-4970
    • (1981) Biochemistry , vol.20 , pp. 4965-4970
    • Mizzer, J.P.1    Thorpe, C.2
  • 34
    • 0031059866 scopus 로고    scopus 로고
    • (Carter, C. W. Jr. and Sweet, R. M. Eds.) pp, Academic Press, San Diego, CA
    • Otwinowski, Z. and Minor, W. (1997) in Macromolecular Crystallography. Part A (Carter, C. W., Jr. and Sweet, R. M., Eds.) pp 307-326, Academic Press, San Diego, CA.
    • (1997) Macromolecular Crystallography. Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 36
    • 0001409925 scopus 로고
    • Role of charge-transfer interactions in flavoprotein catalysis
    • Massey, V. and Ghisla, S. (1974) Role of charge-transfer interactions in flavoprotein catalysis Ann. N.Y. Acad. Sci. 227, 446-465
    • (1974) Ann. N.Y. Acad. Sci. , vol.227 , pp. 446-465
    • Massey, V.1    Ghisla, S.2
  • 37
    • 0041972320 scopus 로고
    • Laser flash photolysis studies of electron transfer between semiquinone and fully reduced free flavins and horse heart cytochrome c
    • Ahmad, I., Cusanovich, M. A., and Tollin, G. (1981) Laser flash photolysis studies of electron transfer between semiquinone and fully reduced free flavins and horse heart cytochrome c Proc. Natl. Acad. Sci. U.S.A. 78, 6724-6728
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 6724-6728
    • Ahmad, I.1    Cusanovich, M.A.2    Tollin, G.3
  • 38
    • 18844452128 scopus 로고    scopus 로고
    • Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme
    • Gao, B. and Ellis, H. R. (2005) Altered mechanism of the alkanesulfonate FMN reductase with the monooxygenase enzyme Biochem. Biophys. Res. Commun. 331, 1137-1145
    • (2005) Biochem. Biophys. Res. Commun. , vol.331 , pp. 1137-1145
    • Gao, B.1    Ellis, H.R.2
  • 39
    • 0346220289 scopus 로고    scopus 로고
    • Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD
    • Kirchner, U., Westphal, A. H., Muller, R., and van Berkel, W. J. (2003) Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD J. Biol. Chem. 278, 47545-47553
    • (2003) J. Biol. Chem. , vol.278 , pp. 47545-47553
    • Kirchner, U.1    Westphal, A.H.2    Muller, R.3    Van Berkel, W.J.4
  • 40
    • 1842424838 scopus 로고    scopus 로고
    • Structural studies on flavin reductase PheA2 reveal binding of FAD in an unusual folded conformation and support novel mechanism of of action
    • van den Heuvel, R. H., Westphal, A. H., Heck, A. J., Walsh, M. A., Rovida, S., van Berkel, W. J., and Mattevi, A. (2004) Structural studies on flavin reductase PheA2 reveal binding of FAD in an unusual folded conformation and support novel mechanism of of action J. Biol. Chem. 279, 12860-12867
    • (2004) J. Biol. Chem. , vol.279 , pp. 12860
    • Van Den Heuvel, R.H.1    Westphal, A.H.2    Heck, A.J.3    Walsh, M.A.4    Rovida, S.5    Van Berkel, W.J.6    Mattevi, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.