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Journal of Biological Inorganic Chemistry
Volumn 14, Issue 8, 2009, Pages 1153-1163
Kinetic and redox properties of MnP II, a major manganese peroxidase isoenzyme from Panus tigrinus CBS 577.79
Author keywords

Direct electron transfer; Manganese peroxidase; Panus tigrinus; Phenols; Purification
Indexed keywords

CONCANAVALIN A; ISOENZYME; MANGANESE PEROXIDASE; MANNOSE; MNP II; PHENOL; SEPHAROSE; UNCLASSIFIED DRUG; VERATRYL ALCOHOL;
EID: 70449530586     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-009-0559-8     Document Type: Article
Times cited : (24)
References (42)
  • 3
    • 0037117763 scopus 로고    scopus 로고
    • Review: Lignin conversion by manganese peroxidase (MnP)
    • DOI 10.1016/S0141-0229(01)00528-2, PII S0141022901005282
    • M Hofrichter 2002 Enzyme Microb Technol 30 454 466 10.1016/S0141-0229(01) 00528-2 1:CAS:528:DC%2BD38Xis1Oru7c%3D (Pubitemid 34326429)
    • (2002) Enzyme and Microbial Technology , vol.30 , Issue.4 , pp. 454-466
    • Hofrichter, M.1
  • 8
    • 0037426673 scopus 로고    scopus 로고
    • Submerged and solid-state production of laccase and Mn-peroxidase by Panus tigrinus on olive mill wastewater-based media
    • DOI 10.1016/S0168-1656(02)00241-9, PII S0168165602002419
    • M Fenice G Giovannozzi Sermanni F Federici A D'Annibale 2003 J Biotechnol 100 77 85 10.1016/S0168-1656(02)00241-9 1:CAS:528:DC%2BD38XotF2is74%3D 12413788 (Pubitemid 35279861)
    • (2003) Journal of Biotechnology , vol.100 , Issue.1 , pp. 77-85
    • Fenice, M.1    Giovannozzi Sermanni, G.2    Federici, F.3    D'Annibale, A.4
  • 10
    • 33845188379 scopus 로고    scopus 로고
    • Enzyme and fungal treatments and a combination thereof reduce olive mill wastewater phytotoxicity on Zea mays L. seeds
    • DOI 10.1016/j.chemosphere.2006.07.092, PII S0045653506010630
    • D Quaratino A D'Annibale F Federici CF Cereti F Rossini 2007 Chemosphere 66 1627 1633 10.1016/j.chemosphere.2006.07.092 1:CAS:528:DC%2BD28XhtlSiu7rN 17007905 (Pubitemid 44855084)
    • (2007) Chemosphere , vol.66 , Issue.9 , pp. 1627-1633
    • Quaratino, D.1    D'Annibale, A.2    Federici, F.3    Cereti, C.F.4    Rossini, F.5    Fenice, M.6
  • 11
    • 4143081761 scopus 로고    scopus 로고
    • Panus tigrinus efficiently removes phenols, color and organic load from olive-mill wastewater
    • DOI 10.1016/j.resmic.2004.04.009, PII S092325080400107X
    • A D'Annibale M Ricci D Quaratino F Federici M Fenice 2004 Res Microbiol 155 596 603 10.1016/j.resmic.2004.04.009 15313262 (Pubitemid 39094213)
    • (2004) Research in Microbiology , vol.155 , Issue.7 , pp. 596-603
    • D'Annibale, A.1    Ricci, M.2    Quaratino, D.3    Federici, F.4    Fenice, M.5
  • 12
    • 0028202957 scopus 로고
    • Production of ligninolytic enzymes of the white rot fungus Panus tigrinus
    • DOI 10.1016/0168-1656(94)90216-X
    • AA Leontievsky NM Myasoedova LA Golovleva 1994 J Biotechnol 32 299 307 10.1016/0168-1656(94)90216-X 1:CAS:528:DyaK2cXktlSlsbc%3D (Pubitemid 24081041)
    • (1994) Journal of Biotechnology , vol.32 , Issue.3 , pp. 299-307
    • Leontievsky, A.A.1
  • 16
    • 4644317336 scopus 로고    scopus 로고
    • Reactions of "hybrid" Mn-peroxidase of the white rot fungus Panus tigrinus with benzylic alcohols in the presence of mediators
    • DOI 10.1016/j.molcatb.2004.06.003, PII S1381117704001894
    • AV Lisov AA Leontievsky LA Golovleva CS Evans 2004 J Mol Catal B Enzym 31 1 8 10.1016/j.molcatb.2004.06.003 1:CAS:528:DC%2BD2cXnvV2rt78%3D (Pubitemid 39297063)
    • (2004) Journal of Molecular Catalysis B: Enzymatic , vol.31 , Issue.1-3 , pp. 1-8
    • Lisov, A.1    Leontievsky, A.2    Golovleva, L.3    Evans, C.4
  • 17
    • 21144442003 scopus 로고    scopus 로고
    • Oxidase reaction of the hybrid Mn-peroxidase of the fungus Panus tigrinus 8/18
    • DOI 10.1007/s10541-005-0138-8
    • AV Lisov AA Leontievsky LA Golovleva 2005 Biochemistry (Mosc) 70 467 472 10.1007/s10541-005-0138-8 1:CAS:528:DC%2BD2MXksVCqsbw%3D (Pubitemid 40878793)
    • (2005) Biochemistry (Moscow) , vol.70 , Issue.4 , pp. 467-472
    • Lisov, A.V.1    Leontievsky, A.A.2    Golovleva, L.A.3
  • 18
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • DOI 10.1002/elps.1150090603
    • V Neuhoff N Arold D Taube W Ehrhardt 1988 Electrophoresis 9 255 262 10.1002/elps.1150090603 1:CAS:528:DyaL1cXksFWisro%3D 2466658 (Pubitemid 18152745)
    • (1988) Electrophoresis , vol.9 , Issue.6 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 19
    • 0027249006 scopus 로고
    • 1:CAS:528:DyaK3sXltlChsL4%3D 8376363
    • IC Kuan K Johnson M Tien 1993 J Biol Chem 268 20064 20070 1:CAS:528:DyaK3sXltlChsL4%3D 8376363
    • (1993) J Biol Chem , vol.268 , pp. 20064-20070
    • Kuan, I.C.1    Johnson, K.2    Tien, M.3
  • 20
    • 0036303386 scopus 로고    scopus 로고
    • 2 production and its impact on manganese peroxidase
    • DOI 10.1128/AEM.68.7.3514-3521.2002
    • D Schlosser C Höfer 2002 Appl Environ Microbiol 68 3514 3521 10.1128/AEM.68.7.3514-3521.2002 1:CAS:528:DC%2BD38Xlt1Sntbs%3D 12089036 (Pubitemid 34734053)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.7 , pp. 3514-3521
    • Schlosser, D.1    Hofer, C.2
  • 21
    • 0003768971 scopus 로고    scopus 로고
    • A.J. Bard L.R. Faulkner (eds). 2 Wiley New York
    • Bard AJ, Faulkner LR (eds) (2002) Electrochemical method, 2nd edn. Wiley, New York
    • (2002) Electrochemical Method
  • 24
    • 49049115593 scopus 로고    scopus 로고
    • 10.1021/cr0680742 18620368
    • C Léger P Bertrand 2008 Chem Rev 108 2379 2438 10.1021/cr0680742 18620368
    • (2008) Chem Rev , vol.108 , pp. 2379-2438
    • Léger, C.1    Bertrand, P.2
  • 25
    • 0025070098 scopus 로고
    • Characterization of reactions catalyzed by manganese peroxidase from Phanerochaete chrysosporium
    • DOI 10.1016/0003-9861(90)90739-L
    • MD Aitken RL Irvine 1990 Arch Biochem Biophys 276 405 414 10.1016/0003-9861(90)90739-L 1:CAS:528:DyaK3cXhslCks7g%3D 2306104 (Pubitemid 20081972)
    • (1990) Archives of Biochemistry and Biophysics , vol.276 , Issue.2 , pp. 405-414
    • Aitken, M.D.1    Irvine, R.L.2
  • 31
    • 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
    • MDS Gelpke HL Youngs MH Gold 2000 Eur J Biochem 267 7038 7045 10.1046/j.1432-1327.2000.01798.x 1:STN:280:DC%2BD3M%2Fos1OrsA%3D%3D 11106414 (Pubitemid 32010758)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.24 , pp. 7038-7045
    • Gelpke, M.D.S.1    Youngs, H.L.2    Gold, M.H.3
  • 32
    • 0032577520 scopus 로고    scopus 로고
    • A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta
    • DOI 10.1016/S0014-5793(98)00512-2, PII S0014579398005122
    • A Heinfling FJ Ruiz-Dueñas MJ Martínez M Bergbauer U Szewzyk AT Martínez 1998 FEBS Lett 428 141 146 10.1016/S0014-5793(98)00512-2 1:CAS:528:DyaK1cXjt1Cmur0%3D 9654123 (Pubitemid 28319673)
    • (1998) FEBS Letters , vol.428 , Issue.3 , pp. 141-146
    • Heinfling, A.1    Ruiz-Duenas, F.J.2    Martinez, M.J.3    Bergbauer, M.4    Szewzyk, U.5    Martinez, A.T.6
  • 33
    • 0033537844 scopus 로고    scopus 로고
    • Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
    • DOI 10.1074/jbc.274.15.10324
    • S Camarero S Sarkar FJ Ruiz-Dueñas MJ Martínez AT Martínez 1999 J Biol Chem 274 10324 10330 10.1074/jbc.274.15.10324 1:CAS:528:DyaK1MXis1GjtbY%3D 10187820 (Pubitemid 29180907)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.15 , pp. 10324-10330
    • Camarero, S.1    Sarkar, S.2    Ruiz-Duenas, F.J.3    Martinez, M.J.4    Martinez, A.T.5
  • 35
    • 0029566344 scopus 로고
    • Lignin peroxidase-type activity of soybean peroxidase
    • DOI 10.1016/0141-0229(94)00060-3
    • JP Mc Eldoon AR Pokora JS Dordick 1995 Enzyme Microb Technol 17 359 365 10.1016/0141-0229(94)00060-3 1:CAS:528:DyaK2MXlsVeisL4%3D (Pubitemid 26032784)
    • (1995) Enzyme and Microbial Technology , vol.17 , Issue.4 , pp. 359-365
    • Dordick, J.S.1
  • 37
    • 0034640371 scopus 로고    scopus 로고
    • The mechanism of the proton transfer: An outline
    • DOI 10.1016/S0005-2728(00)00057-8, PII S0005272800000578
    • LI Krishtalik 2000 Biochim Biophys Acta 1458 6 13 10.1016/S0005-2728(00) 00057-8 1:CAS:528:DC%2BD3cXjsVyqu7g%3D 10812022 (Pubitemid 30254248)
    • (2000) Biochimica et Biophysica Acta - Bioenergetics , vol.1458 , Issue.1 , pp. 6-27
    • Krishtalik, L.I.1
  • 38
    • 33746894166 scopus 로고    scopus 로고
    • Elucidating the mechanisms of coupled electron transfer and catalytic reactions by protein film voltammetry
    • DOI 10.1016/j.bbabio.2006.04.002, PII S0005272806000995
    • J Hirst 2006 Biochim Biophys Acta 1757 225 239 10.1016/j.bbabio.2006.04. 002 1:CAS:528:DC%2BD28XmtVOisLo%3D 16730325 (Pubitemid 44192420)
    • (2006) Biochimica et Biophysica Acta - Bioenergetics , vol.1757 , Issue.4 , pp. 225-239
    • Hirst, J.1
  • 40
    • 0034235415 scopus 로고    scopus 로고
    • Redox equilibria of manganese peroxidase from Phanerochaetes chrysosporium: Functional role of residues on the proximal side of the haem pocket
    • DOI 10.1042/0264-6021:3490085
    • R Santucci C Bongiovanni S Marini R Del Conte M Tien L Banci M Coletta 2000 Biochem J 349 85 90 10.1042/0264-6021:3490085 1:CAS:528: DC%2BD3cXlt1Sgu7k%3D 10861214 (Pubitemid 30440168)
    • (2000) Biochemical Journal , vol.349 , Issue.1 , pp. 85-90
    • Santucci, R.1    Bongiovanni, C.2    Marini, S.3    Del Conte, R.4    Tien, M.5    Banci, L.6    Coletta, M.7

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