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Volumn 36, Issue 7, 2010, Pages 802-815

Peroxidase oxidation of lignin and its model compounds

Author keywords

Catalytic oxidation; Enzymes; Horseradish peroxidase; Laccase; Lignin; Lignin model compoundsl; Lignin peroxidase; Manganese peroxidase

Indexed keywords

ARMORACIA RUSTICANA;

EID: 78650011807     PISSN: 10681620     EISSN: None     Source Type: Journal    
DOI: 10.1134/S1068162010070034     Document Type: Review
Times cited : (15)

References (58)
  • 5
    • 0026825746 scopus 로고
    • 1:CAS:528:DyaK38XlvVKqt7o%3D 1524589
    • M.N. Levit A.M. Shkrob 1992 Bioorg. Khim. 18 3 309 345 1:CAS:528:DyaK38XlvVKqt7o%3D 1524589
    • (1992) Bioorg. Khim. , vol.18 , Issue.3 , pp. 309-345
    • Levit, M.N.1    Shkrob, A.M.2
  • 8
    • 77956368163 scopus 로고
    • D.N.-S. Hon N. Shiraishi (eds). Mercek Dekker New York
    • Shimada, M. and Higuchi, L., in Wood and Cellulosic Chemistry, Hon, D.N.-S. and Shiraishi, N., Eds., New York: Mercek Dekker, 1991, pp. 525-591.
    • (1991) Wood and Cellulosic Chemistry , pp. 525-591
    • Shimada, M.1    Higuchi, L.2
  • 11
    • 0017186887 scopus 로고
    • 1:CAS:528:DyaE28Xlslens7g%3D 9411
    • W.D. Hewson H.B. Dunford 1976 J. Biol. Chem. 251 19 6036 6042 1:CAS:528:DyaE28Xlslens7g%3D 9411
    • (1976) J. Biol. Chem. , vol.251 , Issue.19 , pp. 6036-6042
    • Hewson, W.D.1    Dunford, H.B.2
  • 13
    • 0027158797 scopus 로고
    • 1:CAS:528:DyaK3sXktVeqs7Y%3D 10.1021/bi00073a015 8504102
    • L. Banci I. Bertini T. Bini, et al. 1993 Biochemistry 32 22 5825 5831 1:CAS:528:DyaK3sXktVeqs7Y%3D 10.1021/bi00073a015 8504102
    • (1993) Biochemistry , vol.32 , Issue.22 , pp. 5825-5831
    • Banci, L.1    Bertini, I.2    Bini, T.3
  • 14
    • 0032042908 scopus 로고    scopus 로고
    • 1:CAS:528:DyaK1cXjs1OltLg%3D 10.1016/S1367-5931(98)80069-0 9667928
    • A.T. Smith N.C. Veitch 1998 Curr. Opin. Chem. Biol. 2 269 278 1:CAS:528:DyaK1cXjs1OltLg%3D 10.1016/S1367-5931(98)80069-0 9667928
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 269-278
    • Smith, A.T.1    Veitch, N.C.2
  • 15
    • 0000355605 scopus 로고
    • 1:CAS:528:DyaL2MXktlCis7Y%3D 10.1021/bi00335a002
    • D. Kuila M. Tien J.A. Fee M.R. Ondrias 1985 Biochemistry 24 3394 3397 1:CAS:528:DyaL2MXktlCis7Y%3D 10.1021/bi00335a002
    • (1985) Biochemistry , vol.24 , pp. 3394-3397
    • Kuila, D.1    Tien, M.2    Fee, J.A.3    Ondrias, M.R.4
  • 16
    • 0021844391 scopus 로고
    • 1:CAS:528:DyaL2MXktF2jtrk%3D 2987213
    • L.A. Andersson V. Renganathan A. Chiu, et al. 1985 J. Biol. Chem. 260 10 6080 6087 1:CAS:528:DyaL2MXktF2jtrk%3D 2987213
    • (1985) J. Biol. Chem. , vol.260 , Issue.10 , pp. 6080-6087
    • Andersson, L.A.1    Renganathan, V.2    Chiu, A.3
  • 17
    • 0023661643 scopus 로고
    • 1:CAS:528:DyaL2sXhslWqs74%3D 10.1021/bi00382a028 3040086
    • L.A. Andersson V. Renganathan T.M. Loehr, et al. 1987 Biochemistry 26 8 2258 2263 1:CAS:528:DyaL2sXhslWqs74%3D 10.1021/bi00382a028 3040086
    • (1987) Biochemistry , vol.26 , Issue.8 , pp. 2258-2263
    • Andersson, L.A.1    Renganathan, V.2    Loehr, T.M.3
  • 21
    • 0022962952 scopus 로고
    • 1:CAS:528:DyaL2sXhtlChsb0%3D 10.1016/0003-9861(86)90361-9 3800384
    • H.B. Dunford A.J. Adeniran 1986 Arch. Biochem. Biophys. 251 536 542 1:CAS:528:DyaL2sXhtlChsb0%3D 10.1016/0003-9861(86)90361-9 3800384
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 536-542
    • Dunford, H.B.1    Adeniran, A.J.2
  • 24
    • 0034003801 scopus 로고    scopus 로고
    • The reactivity of phenolic and non-phenolic residual kraft lignin model compounds with Mn(II)-peroxidase from Lentinula edodes
    • DOI 10.1016/S0968-0896(99)00303-X, PII S096808969900303X
    • C. Crestini A. DAnnibale G.G. Sermanni R. Saladino 2000 Bioorg. Med. Chem. 8 2 433 438 1:CAS:528:DC%2BD3cXhsVWksbk%3D 10.1016/S0968-0896(99)00303-X 10722166 (Pubitemid 30122784)
    • (2000) Bioorganic and Medicinal Chemistry , vol.8 , Issue.2 , pp. 433-438
    • Crestini, C.1    D'Annibale, A.2    Sermanni, G.G.3    Saladino, R.4
  • 25
    • 0034535788 scopus 로고    scopus 로고
    • II binding site of manganese peroxidase: Studies with R177D, R177E, R177N, and R177Q mutants
    • DOI 10.1046/j.1432-1327.2000.01798.x
    • M.D.S. Gelpke H.L. Youngs M.N. Gold 2000 Eur. J. Biochem. 267 7038 7054 1:STN:280:DC%2BD3M%2Fos1OrsA%3D%3D 10.1046/j.1432-1327.2000.01798.x 11106414 (Pubitemid 32010758)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.24 , pp. 7038-7045
    • Sollewijn Gelpke, M.D.1    Youngs, H.L.2    Gold, M.H.3
  • 27
    • 0001007398 scopus 로고
    • 1:CAS:528:DyaL28Xjt1Gr 10.1016/S0031-9422(00)80667-6
    • I. Marbach E. Harel A.M. Mayer 1985 Phytochemistry 24 2559 2561 1:CAS:528:DyaL28Xjt1Gr 10.1016/S0031-9422(00)80667-6
    • (1985) Phytochemistry , vol.24 , pp. 2559-2561
    • Marbach, I.1    Harel, E.2    Mayer, A.M.3
  • 28
    • 0030614462 scopus 로고    scopus 로고
    • The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression
    • DOI 10.1074/jbc.272.2.705
    • F. Xu 1997 J. Biol. Chem. 272 2 924 928 1:CAS:528:DyaK2sXmtFGjsw%3D%3D 10.1074/jbc.272.2.705 8995383 (Pubitemid 27035012)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.2 , pp. 705-708
    • Li, X.1    Xu, J.2    Li, M.3
  • 29
    • 0000230699 scopus 로고
    • 1:CAS:528:DyaL2cXksFSmt7s%3D 10.1073/pnas.81.8.2280 16593451
    • M. Tien T.K. Kirk 1984 Proc. Natl. Acad. Sci. USA 81 8 2280 2284 1:CAS:528:DyaL2cXksFSmt7s%3D 10.1073/pnas.81.8.2280 16593451
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , Issue.8 , pp. 2280-2284
    • Tien, M.1    Kirk, T.K.2
  • 30
    • 0000355605 scopus 로고
    • 1:CAS:528:DyaL2MXktlCis7Y%3D 10.1021/bi00335a002
    • D. Kuila M. Tien J.A. Fee M.R. Ondrias 1985 Biochemistry 24 14 3394 3397 1:CAS:528:DyaL2MXktlCis7Y%3D 10.1021/bi00335a002
    • (1985) Biochemistry , vol.24 , Issue.14 , pp. 3394-3397
    • Kuila, D.1    Tien, M.2    Fee, J.A.3    Ondrias, M.R.4
  • 31
    • 0024864423 scopus 로고
    • 1:CAS:528:DyaL1MXktVejs74%3D 10.1021/bk-1989-0389.ch009
    • M.H. Gold H. Wariishi K. Valli 1989 ACS Symp. Ser. 389 127 140 1:CAS:528:DyaL1MXktVejs74%3D 10.1021/bk-1989-0389.ch009
    • (1989) ACS Symp. Ser. , vol.389 , pp. 127-140
    • Gold, M.H.1    Wariishi, H.2    Valli, K.3
  • 33
    • 0025119879 scopus 로고
    • Characterization of a gene encoding a manganese peroxidase from Phanerochaete chrysosporium
    • DOI 10.1016/0378-1119(90)90144-G
    • B.J. Godfrey M.B. Mayfield J.A. Brown M.H. Gold 1990 Gene 93 1 119 124 1:CAS:528:DyaK3MXhsFyit7o%3D 10.1016/0378-1119(90)90144-G 2227420 (Pubitemid 20353091)
    • (1990) Gene , vol.93 , Issue.1 , pp. 119-124
    • Godfrey, B.J.1    Mayfield, M.B.2    Brown, J.A.3    Gold, M.H.4
  • 34
    • 0022522916 scopus 로고
    • 1:CAS:528:DyaL28XhsVCmtLs%3D 10.1021/bi00355a027
    • V. Renganathan M.H. Gold 1986 Biochemistry 25 7 1626 1631 1:CAS:528:DyaL28XhsVCmtLs%3D 10.1021/bi00355a027
    • (1986) Biochemistry , vol.25 , Issue.7 , pp. 1626-1631
    • Renganathan, V.1    Gold, M.H.2
  • 35
    • 0344939469 scopus 로고
    • 1:CAS:528:DyaF2cXktFags70%3D 14209968
    • L. Dure M.J. Cormier 1964 J. Biol. Chem. 239 2351 2359 1:CAS:528:DyaF2cXktFags70%3D 14209968
    • (1964) J. Biol. Chem. , vol.239 , pp. 2351-2359
    • Dure, L.1    Cormier, M.J.2
  • 36
    • 0022974689 scopus 로고
    • 1:CAS:528:DyaL28XhtVGjs7w%3D 3003081
    • M. Tien T. Kirk C. Bull J.A. Fee 1986 J. Biol. Chem. 261 4 1687 1693 1:CAS:528:DyaL28XhtVGjs7w%3D 3003081
    • (1986) J. Biol. Chem. , vol.261 , Issue.4 , pp. 1687-1693
    • Tien, M.1    Kirk, T.2    Bull, C.3    Fee, J.A.4
  • 37
    • 0022389495 scopus 로고
    • Purification and characterization of an extracellular Mn(II)-dependent peroxidase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium
    • DOI 10.1016/0003-9861(85)90217-6
    • J.K. Glenn M.H. Gold 1985 Arch. Biochem. Biophys. 242 2 329 341 1:CAS:528:DyaL28XisFKr 10.1016/0003-9861(85)90217-6 4062285 (Pubitemid 16217486)
    • (1985) Archives of Biochemistry and Biophysics , vol.242 , Issue.2 , pp. 329-341
    • Glenn, J.K.1    Gold, M.H.2
  • 39
    • 0021992631 scopus 로고
    • On the mechanism of enzymatic lignin breakdown
    • DOI 10.1016/0014-5793(85)80942-X
    • H.E. Schoemaker P.J. Harvey R.M. Bowen J.M. Palmer 1985 FEBS Lett. 183 1 7 12 1:CAS:528:DyaL2MXitFKqtbw%3D 10.1016/0014-5793(85)80942-X (Pubitemid 15090118)
    • (1985) FEBS Letters , vol.183 , Issue.1 , pp. 7-12
    • Schoemaker, H.E.1    Harvey, P.J.2    Bowen, R.M.3    Palmer, J.M.4
  • 44
    • 0029046914 scopus 로고
    • 1:CAS:528:DyaK2MXlt1Cmt78%3D 10.1021/bi00018a003 7742304
    • A. Khindaria T.A. Grover S.D. Aust 1995 Biochemistry 34 6020 6025 1:CAS:528:DyaK2MXlt1Cmt78%3D 10.1021/bi00018a003 7742304
    • (1995) Biochemistry , vol.34 , pp. 6020-6025
    • Khindaria, A.1    Grover, T.A.2    Aust, S.D.3
  • 45
    • 0029160709 scopus 로고
    • 1:CAS:528:DyaK2MXot1GhsLg%3D 10.1074/jbc.270.38.22254 7673205
    • R.S. Koduri M. Tien 1995 J. Biol. Chem. 270 38 22254 22258 1:CAS:528:DyaK2MXot1GhsLg%3D 10.1074/jbc.270.38.22254 7673205
    • (1995) J. Biol. Chem. , vol.270 , Issue.38 , pp. 22254-22258
    • Koduri, R.S.1    Tien, M.2
  • 46
    • 0037073011 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD38Xms1yntbw%3D 10.1016/S1381-1177(02)00074-7
    • J.A. Laszlo D.L. Compton 2002 J. Mol. Cat. B 18 109 120 1:CAS:528:DC%2BD38Xms1yntbw%3D 10.1016/S1381-1177(02)00074-7
    • (2002) J. Mol. Cat. B , vol.18 , pp. 109-120
    • Laszlo, J.A.1    Compton, D.L.2
  • 47
    • 0035811944 scopus 로고    scopus 로고
    • Inactivation of lignin peroxidase during oxidation of the highly reactive substrate ferulic acid
    • DOI 10.1016/S0141-0229(01)00336-2, PII S0141022901003362
    • G. Ward Y. Hadar C.G. Dosoretz 2001 Enzyme Microb. Technol. 29 1 34 41 1:CAS:528:DC%2BD3MXks1Ols7c%3D 10.1016/S0141-0229(01)00336-2 11427233 (Pubitemid 32566383)
    • (2001) Enzyme and Microbial Technology , vol.29 , Issue.1 , pp. 34-41
    • Ward, G.1    Hadar, Y.2    Dosoretz, C.G.3
  • 52
    • 0009092316 scopus 로고
    • 1:CAS:528:DyaL1MXhvFCrur4%3D 10.1016/0144-8617(89)90029-5
    • R.H. Hwang J.F. Kennedy E.H.M. Melo 1989 Carbohydrate Polymers 10 1 15 30 1:CAS:528:DyaL1MXhvFCrur4%3D 10.1016/0144-8617(89)90029-5
    • (1989) Carbohydrate Polymers , vol.10 , Issue.1 , pp. 15-30
    • Hwang, R.H.1    Kennedy, J.F.2    Melo, E.H.M.3
  • 53
    • 0025045521 scopus 로고
    • Influence of the physical state of lignin on its degradability by the lignin peroxidase of Phanerochaete chrysosporium
    • DOI 10.1016/0141-0229(90)90150-O
    • B. Kurek B. Monties E. Odier 1990 Enzyme Microb. Technol. 12 10 771 777 1:CAS:528:DyaK3cXmtVOhtbk%3D 10.1016/0141-0229(90)90150-O (Pubitemid 20303116)
    • (1990) Enzyme and Microbial Technology , vol.12 , Issue.10 , pp. 771-777
    • Kurek, B.1    Monties, B.2    Odier, E.3
  • 54
    • 0026010999 scopus 로고
    • 1:CAS:528:DyaK3MXlvVShtw%3D%3D 10.1016/0141-0229(91)90182-A
    • K.E. Hammel M.A. Moen 1991 Enzyme Microb. Technol. 13 1 15 18 1:CAS:528:DyaK3MXlvVShtw%3D%3D 10.1016/0141-0229(91)90182-A
    • (1991) Enzyme Microb. Technol. , vol.13 , Issue.1 , pp. 15-18
    • Hammel, K.E.1    Moen, M.A.2
  • 55
    • 0035798657 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD3MXosVKhtbg%3D 10.1074/jbc.M107489200 11546788
    • B.D. Howes A. Feis L. Raimondi G. Smulevich 2001 J. Biol. Chem. 276 44 40704 40711 1:CAS:528:DC%2BD3MXosVKhtbg%3D 10.1074/jbc.M107489200 11546788
    • (2001) J. Biol. Chem. , vol.276 , Issue.44 , pp. 40704-40711
    • Howes, B.D.1    Feis, A.2    Raimondi, L.3    Smulevich, G.4
  • 56
    • 0000707433 scopus 로고
    • 1:CAS:528:DyaF3sXkslKgur4%3D 14109213
    • M. Klapper D.P. Hackett 1963 J. Biol. Chem. 238 11 3736 3742 1:CAS:528:DyaF3sXkslKgur4%3D 14109213
    • (1963) J. Biol. Chem. , vol.238 , Issue.11 , pp. 3736-3742
    • Klapper, M.1    Hackett, D.P.2


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