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Volumn 87, Issue 5, 2010, Pages 1595-1603

Dioxygen activation responsible for oxidation of aliphatic and aromatic hydrocarbon compounds: Current state and variants

Author keywords

Alkane monooxygenase; Hydrocarbon; Naphthalene dioxygenase; Oxygenase; P450; Rieske dioxygenase

Indexed keywords

ALKANE MONOOXYGENASE; DIOXYGENASES; MONOOXYGENASES; NAPHTHALENE DIOXYGENASE; OXYGENASES;

EID: 77955555124     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-010-2715-z     Document Type: Short Survey
Times cited : (21)

References (34)
  • 2
    • 70349776273 scopus 로고    scopus 로고
    • Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase
    • 10.1021/bi901150a 1:CAS:528:DC%2BD1MXhtVOgu77N
    • LJ Bailey BG Fox 2009 Crystallographic and catalytic studies of the peroxide-shunt reaction in a diiron hydroxylase Biochemistry 48 8932 8939 10.1021/bi901150a 1:CAS:528:DC%2BD1MXhtVOgu77N
    • (2009) Biochemistry , vol.48 , pp. 8932-8939
    • Bailey, L.J.1    Fox, B.G.2
  • 3
    • 34547752024 scopus 로고    scopus 로고
    • Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase
    • 10.1021/ar700004s 1:CAS:528:DC%2BD2sXksFartb8%3D
    • R Balasubramanian AC Rosenzweig 2007 Structural and mechanistic insights into methane oxidation by particulate methane monooxygenase Acc Chem Res 40 573 580 10.1021/ar700004s 1:CAS:528:DC%2BD2sXksFartb8%3D
    • (2007) Acc Chem Res , vol.40 , pp. 573-580
    • Balasubramanian, R.1    Rosenzweig, A.C.2
  • 4
    • 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
    • DP Ballou B Entsch LJ Cole 2005 Dynamics involved in catalysis by single-component and two-component flavin-dependent aromatic hydroxylases Biochem Biophys Res Commun 338 590 598 10.1016/j.bbrc.2005.09.081 1:CAS:528:DC%2BD2MXhtFyksrvK (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
  • 5
    • 9244231291 scopus 로고    scopus 로고
    • Biophysical analyses of designed and selected mutants of protocatechuate 3,4-dioxygenase
    • DOI 10.1146/annurev.micro.57.030502.090927
    • CK Brown MW Vetting CA Earhart DH Ohlendorf 2004 Biophysical analyses of designed and selected mutants of protocatechuate 3, 4-dioxygenase1 Annu Rev Microbiol 58 555 585 10.1146/annurev.micro.57.030502.090927 1:CAS:528: DC%2BD2cXhtVejsr3N (Pubitemid 39551997)
    • (2004) Annual Review of Microbiology , vol.58 , pp. 555-585
    • Brown, C.K.1    Vetting, M.W.2    Earhart, C.A.3    Ohlendorf, D.H.4
  • 6
    • 43049091488 scopus 로고    scopus 로고
    • Non-heme iron-dependent dioxygenases: Unravelling catalytic mechanisms for complex enzymatic oxidations
    • 10.1016/j.cbpa.2007.12.007 1:CAS:528:DC%2BD1cXlslKlsLk%3D
    • TD Bugg S Ramaswamy 2008 Non-heme iron-dependent dioxygenases: unravelling catalytic mechanisms for complex enzymatic oxidations Curr Opin Chem Biol 12 134 140 10.1016/j.cbpa.2007.12.007 1:CAS:528:DC%2BD1cXlslKlsLk%3D
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 134-140
    • Bugg, T.D.1    Ramaswamy, S.2
  • 7
    • 0031720708 scopus 로고    scopus 로고
    • Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1
    • 1:CAS:528:DyaK1cXlvVCmu7w%3D
    • BM Bundy AL Campbell EL Neidle 1998 Similarities between the antABC-encoded anthranilate dioxygenase and the benABC-encoded benzoate dioxygenase of Acinetobacter sp. strain ADP1 J Bacteriol 180 4466 4474 1:CAS:528:DyaK1cXlvVCmu7w%3D
    • (1998) J Bacteriol , vol.180 , pp. 4466-4474
    • Bundy, B.M.1    Campbell, A.L.2    Neidle, E.L.3
  • 8
    • 16244423655 scopus 로고    scopus 로고
    • Dioxygen activation by copper, heme and non-heme iron enzymes: Comparison of electronic structures and reactivities
    • DOI 10.1016/j.cbpa.2005.02.012, Bioorganic Chemistry / Biocatalysis and Biotransformation
    • A Decker EI Solomon 2005 Dioxygen activation by copper, heme and non-heme iron enzymes: comparison of electronic structures and reactivities Curr Opin Chem Biol 9 152 163 10.1016/j.cbpa.2005.02.012 1:CAS:528:DC%2BD2MXivFSlsr8%3D (Pubitemid 40462484)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.2 , pp. 152-163
    • Decker, A.1    Solomon, E.I.2
  • 9
    • 0034096459 scopus 로고    scopus 로고
    • Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily
    • 10.1128/MMBR.64.1.153-179.2000 1:CAS:528:DC%2BD3cXitFygsrw%3D
    • JM Dunwell S Khuri PJ Gane 2000 Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily Microbiol Mol Biol Rev 64 153 179 10.1128/MMBR.64.1.153-179.2000 1:CAS:528:DC%2BD3cXitFygsrw%3D
    • (2000) Microbiol Mol Biol Rev , vol.64 , pp. 153-179
    • Dunwell, J.M.1    Khuri, S.2    Gane, P.J.3
  • 11
    • 0347264753 scopus 로고    scopus 로고
    • Crystal structure of naphthalene dioxygenase: Side-on binding of dioxygen to iron
    • DOI 10.1126/science.1078020
    • A Karlsson JV Parales RE Parales DT Gibson H Eklund S Ramaswamy 2003 Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron Science 299 1039 1042 10.1126/science.1078020 1:CAS:528: DC%2BD3sXhtFarsLg%3D (Pubitemid 36222924)
    • (2003) Science , vol.299 , Issue.5609 , pp. 1039-1042
    • Karlsson, A.1    Parales, J.V.2    Parales, R.E.3    Gibson, D.T.4    Eklund, H.5    Ramaswamy, S.6
  • 12
    • 17644413773 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad: A versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes
    • DOI 10.1007/s00775-005-0624-x
    • KD Koehntop JP Emerson L Que Jr 2005 The 2-His-1-carboxylate facial triad: a versatile platform for dioxygen activation by mononuclear non-heme iron(II) enzymes J Biol Inorg Chem 10 87 93 10.1007/s00775-005-0624-x 1:CAS:528:DC%2BD2MXjtVWmtLw%3D (Pubitemid 40569003)
    • (2005) Journal of Biological Inorganic Chemistry , vol.10 , Issue.2 , pp. 87-93
    • Koehntop, K.D.1    Emerson, J.P.2    Que Jr., L.3
  • 13
    • 39449130475 scopus 로고    scopus 로고
    • Versatility of biological non-heme Fe(II) centers in oxygen activation reactions
    • DOI 10.1038/nchembio.71, PII NCHEMBIO71
    • EG Kovaleva JD Lipscomb 2008 Versatility of biological non-heme Fe(II) centers in oxygen activation reactions Nat Chem Biol 4 186 93 10.1038/nchembio.71 1:CAS:528:DC%2BD1cXitVGlu7c%3D (Pubitemid 351265327)
    • (2008) Nature Chemical Biology , vol.4 , Issue.3 , pp. 186-193
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 14
    • 0141448799 scopus 로고    scopus 로고
    • Evolution of the soluble diiron monooxygenases
    • DOI 10.1016/S0168-6445(03)00023-8
    • JG Leahy PJ Batchelor SM Morcomb 2003 Evolution of the soluble diiron monooxygenases FEMS Microbiol Rev 27 449 479 10.1016/S0168-6445(03)00023-8 1:CAS:528:DC%2BD3sXnvFShtbc%3D (Pubitemid 37205164)
    • (2003) FEMS Microbiology Reviews , vol.27 , Issue.4 , pp. 449-479
    • Leahy, J.G.1    Batchelor, P.J.2    Morcomb, S.M.3
  • 15
    • 38349124762 scopus 로고    scopus 로고
    • Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: Unveiling the long-chain alkane hydroxylase
    • 10.1016/j.jmb.2007.11.069 1:CAS:528:DC%2BD1cXhtV2nsL4%3D
    • L Li X Liu W Yang F Xu W Wang L Feng M Bartlam L Wang Z Rao 2008 Crystal structure of long-chain alkane monooxygenase (LadA) in complex with coenzyme FMN: unveiling the long-chain alkane hydroxylase J Mol Biol 376 453 465 10.1016/j.jmb.2007.11.069 1:CAS:528:DC%2BD1cXhtV2nsL4%3D
    • (2008) J Mol Biol , vol.376 , pp. 453-465
    • Li, L.1    Liu, X.2    Yang, W.3    Xu, F.4    Wang, W.5    Feng, L.6    Bartlam, M.7    Wang, L.8    Rao, Z.9
  • 16
    • 57049146277 scopus 로고    scopus 로고
    • Mechanism of extradiol aromatic ring-cleaving dioxygenases
    • 10.1016/j.sbi.2008.11.001 1:CAS:528:DC%2BD1cXhsVOisr7N
    • JD Lipscomb 2008 Mechanism of extradiol aromatic ring-cleaving dioxygenases Curr Opin Struct Biol 18 644 649 10.1016/j.sbi.2008.11.001 1:CAS:528:DC%2BD1cXhsVOisr7N
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 644-649
    • Lipscomb, J.D.1
  • 17
    • 70350686084 scopus 로고    scopus 로고
    • Molecular characterization of the alkB gene in the thermophilic Geobacillus sp. strain MH-1
    • 10.1016/j.resmic.2009.08.010 1:CAS:528:DC%2BD1MXhtlCms7rP
    • YC Liu TT Zhou J Zhang L Xu ZH Zhang QR Shen B Shen 2009 Molecular characterization of the alkB gene in the thermophilic Geobacillus sp. strain MH-1 Res Microbiol 160 560 566 10.1016/j.resmic.2009.08.010 1:CAS:528: DC%2BD1MXhtlCms7rP
    • (2009) Res Microbiol , vol.160 , pp. 560-566
    • Liu, Y.C.1    Zhou, T.T.2    Zhang, J.3    Xu, L.4    Zhang, Z.H.5    Shen, Q.R.6    Shen, B.7
  • 18
    • 33846356640 scopus 로고    scopus 로고
    • Cytochrome P450-redox partner fusion enzymes
    • 1:CAS:528:DC%2BD2sXpvVyqtw%3D%3D
    • AW Munro HM Girvan KJ McLean 2007 Cytochrome P450-redox partner fusion enzymes Biochim Biophys Acta 1770 345 359 1:CAS:528:DC%2BD2sXpvVyqtw%3D%3D
    • (2007) Biochim Biophys Acta , vol.1770 , pp. 345-359
    • Munro, A.W.1    Girvan, H.M.2    McLean, K.J.3
  • 19
    • 29644443792 scopus 로고    scopus 로고
    • Structure-function correlations in oxygen activating non-heme iron enzymes
    • Neidig ML, Solomon EI (2005) Structure-function correlations in oxygen activating non-heme iron enzymes. Chem Commun 47:5843-5863
    • (2005) Chem Commun , vol.47 , pp. 5843-5863
    • Neidig, M.L.1    Solomon, E.I.2
  • 20
    • 0029416969 scopus 로고
    • Di-iron-carboxylate proteins
    • 10.1016/0959-440X(95)80008-5 1:CAS:528:DyaK28XkvVCh
    • P Nordlund H Eklund 1995 Di-iron-carboxylate proteins Curr Opin Struct Biol 5 758 766 10.1016/0959-440X(95)80008-5 1:CAS:528:DyaK28XkvVCh
    • (1995) Curr Opin Struct Biol , vol.5 , pp. 758-766
    • Nordlund, P.1    Eklund, H.2
  • 21
    • 0037826062 scopus 로고    scopus 로고
    • The role of active-site residues in naphthalene dioxygenase
    • DOI 10.1007/s10295-003-0043-3
    • RE Parales 2003 The role of active-site residues in naphthalene dioxygenase J Ind Microbiol Biotechnol 30 271 278 10.1007/s10295-003-0043-3 1:CAS:528:DC%2BD3sXltFCntbo%3D (Pubitemid 36870613)
    • (2003) Journal of Industrial Microbiology and Biotechnology , vol.30 , Issue.5 , pp. 271-278
    • Parales, R.E.1
  • 22
    • 0001367075 scopus 로고
    • Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain
    • 10.1016/0006-291X(64)90171-8
    • JS Rieske DH Maclennan R Coleman 1964 Isolation and properties of an iron-protein from the (reduced coenzyme Q)-cytochrome C reductase complex of the respiratory chain Biochem Biophys Res Commun 15 338 344 10.1016/0006-291X(64) 90171-8
    • (1964) Biochem Biophys Res Commun , vol.15 , pp. 338-344
    • Rieske, J.S.1    MacLennan, D.H.2    Coleman, R.3
  • 23
    • 1542571790 scopus 로고    scopus 로고
    • A Self-sufficient Cytochrome P450 with a primary structural organization that includes a Flavin Domain and a [2Fe-2S] Redox Center
    • 10.1074/jbc.M309630200 1:CAS:528:DC%2BD3sXptlGku74%3D
    • GA Roberts A Celik DJ Hunter TW Ost JH White SK Chapman NJ Turner SL Flitsch 2003 A Self-sufficient Cytochrome P450 with a primary structural organization that includes a Flavin Domain and a [2Fe-2S] Redox Center J Biol Chem 278 48914 48920 10.1074/jbc.M309630200 1:CAS:528:DC%2BD3sXptlGku74%3D
    • (2003) J Biol Chem , vol.278 , pp. 48914-48920
    • Roberts, G.A.1    Celik, A.2    Hunter, D.J.3    Ost, T.W.4    White, J.H.5    Chapman, S.K.6    Turner, N.J.7    Flitsch, S.L.8
  • 24
    • 59149098424 scopus 로고    scopus 로고
    • The metal centres of particulate methane mono-oxygenase
    • 10.1042/BST0361134 1:CAS:528:DC%2BD1cXhsVCgsLnE
    • AC Rosenzweig 2008 The metal centres of particulate methane mono-oxygenase Biochem Soc Trans 36 1134 1137 10.1042/BST0361134 1:CAS:528:DC%2BD1cXhsVCgsLnE
    • (2008) Biochem Soc Trans , vol.36 , pp. 1134-1137
    • Rosenzweig, A.C.1
  • 25
    • 34548836830 scopus 로고    scopus 로고
    • Molecular Mechanism of the Redox-dependent Interaction between NADH-dependent Ferredoxin Reductase and Rieske-type [2Fe-2S] Ferredoxin
    • DOI 10.1016/j.jmb.2007.08.002, PII S0022283607010583
    • M Senda S Kishigami S Kimura M Fukuda T Ishida T Senda 2007 Molecular mechanism of the redox-dependent interaction between NADH-dependent ferredoxin reductase and Rieske-type [2Fe-2S] ferredoxin J Mol Biol 373 382 400 10.1016/j.jmb.2007.08.002 1:CAS:528:DC%2BD2sXhtFSksrfF (Pubitemid 47445576)
    • (2007) Journal of Molecular Biology , vol.373 , Issue.2 , pp. 382-400
    • Senda, M.1    Kishigami, S.2    Kimura, S.3    Fukuda, M.4    Ishida, T.5    Senda, T.6
  • 26
    • 0037168426 scopus 로고    scopus 로고
    • Anaerobic enzymesubstrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2,3-dioxygenase
    • DOI 10.1073/pnas.262506299
    • RA Steiner KH Kalk BW Dijkstra 2002 Anaerobic enzyme substrate structures provide insight into the reaction mechanism of the copper-dependent quercetin 2, 3-dioxygenase Proc Natl Acad Sci 99 16625 16630 10.1073/pnas.262506299 1:CAS:528:DC%2BD3sXhvVyqug%3D%3D (Pubitemid 36034023)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.26 , pp. 16625-16630
    • Steiner, R.A.1    Kalk, K.H.2    Dijkstrat, B.W.3
  • 27
    • 34249658423 scopus 로고    scopus 로고
    • Identification of novel genes involved in long-chain n-alkane degradation by Acinetobacter sp. strain DSM 17874
    • DOI 10.1128/AEM.00064-07
    • M Throne-Holst A Wentzel TE Ellingsen H-K Kotlar SB Zotchev 2007 Identification of novel genes involved in long-chain n-alkane degradation by Acinetobacter sp. strain DSM17874 Appl Environ Microbiol 73 3327 3332 10.1128/AEM.00064-07 1:CAS:528:DC%2BD2sXlslSnu7c%3D (Pubitemid 46834985)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.10 , pp. 3327-3332
    • Throne-Holst, M.1    Wentzel, A.2    Ellingsen, T.E.3    Kotlar, H.-K.4    Zotchev, S.B.5
  • 28
    • 0036118468 scopus 로고    scopus 로고
    • Ferredoxin-mediated reactivation of the chlorocatechol 2,3-dioxygenase from Pseudomonas putida GJ31
    • DOI 10.1007/s00203-002-0399-1
    • D Tropel C Meyer Y Jouanneau 2002 Ferredoxin-mediated reactivation of the chlorocatechol 2, 3-dioxygenase from Pseudomonas putida GJ31 Arch Microbiol 177 345 351 10.1007/s00203-002-0399-1 1:CAS:528:DC%2BD38XjtFKqt7g%3D (Pubitemid 34230672)
    • (2002) Archives of Microbiology , vol.177 , Issue.4 , pp. 345-351
    • Tropel, D.1    Meyer, C.2    Armengaud, J.3    Jouanneau, Y.4
  • 29
  • 30
    • 11144307432 scopus 로고    scopus 로고
    • Identification of an amino acid position that determines the substrate range of integral membrane alkane hydroxylases
    • DOI 10.1128/JB.187.1.85-91.2005
    • JB van Beilen TH Smits FF Roos T Brunner SB Balada M Röthlisberger B Witholt 2005 Identification of an amino acid position that determines the substrate range of integral membrane alkane hydroxylases J Bacteriol 187 85 91 10.1128/JB.187.1.85-91.2005 (Pubitemid 40024183)
    • (2005) Journal of Bacteriology , vol.187 , Issue.1 , pp. 85-91
    • Van Beilen, J.B.1    Smits, T.H.M.2    Roos, F.F.3    Brunner, T.4    Balada, S.B.5    Rothlisberger, M.6    Witholt, B.7
  • 32
    • 33846621913 scopus 로고    scopus 로고
    • Alkane hydroxylases involved in microbial alkane degradation
    • DOI 10.1007/s00253-006-0748-0
    • JB van Beilen EG Funhoff 2007 Alkane hydroxylases involved in microbial alkane degradation Appl Microbiol Biotechnol 74 13 21 10.1007/s00253-006-0748-0 1:CAS:528:DC%2BD2sXhtVansLg%3D (Pubitemid 46183463)
    • (2007) Applied Microbiology and Biotechnology , vol.74 , Issue.1 , pp. 13-21
    • Van Beilen, J.B.1    Funhoff, E.G.2
  • 33
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • DOI 10.1016/j.jbiotec.2006.03.044, PII S016816560600318X
    • WJ van Berkel NM Kamerbeek MW Fraaije 2006 Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts J Biotechnol 124 670 689 10.1016/j.jbiotec.2006.03.044 (Pubitemid 44066596)
    • (2006) Journal of Biotechnology , vol.124 , Issue.4 , pp. 670-689
    • Van Berkel, W.J.H.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 34
    • 0020358121 scopus 로고
    • Subunit structure of oxygenase component in benzoate-1, 2-dioxygenase system from Pseudomonas arvilla C-1
    • 1:CAS:528:DyaL38XlslOrs78%3D
    • M Yamaguchi H Fujisawa 1982 Subunit structure of oxygenase component in benzoate-1, 2-dioxygenase system from Pseudomonas arvilla C-1 J Biol Chem 257 12497 12502 1:CAS:528:DyaL38XlslOrs78%3D
    • (1982) J Biol Chem , vol.257 , pp. 12497-12502
    • Yamaguchi, M.1    Fujisawa, H.2


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