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The DOI matches its Crossref record; 183 of the 183 references it cites were found in a registry or an index.

Structure and Action Mechanism of Ligninolytic Enzymes

Wong, Dominic W. S.·2009·Applied Biochemistry and Biotechnology
DOI 10.1007/s12010-008-8279-z
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Show all 183 references

Research works printed but not linked: 28

  1. Fukushima, K. (2001). Regulation of syringyl to guaiacyl ratio in lignin biosynthesis. Journal of Plant Research, 114, 499–508, doi: 10.1007/PL00014017 . · doi:10.1007/pl00014017
  2. Brauns, F. E. (1939). Native lignin I. Its isolation and methylation. Journal of the American Chemical Society, 61, 2120–2127, doi: 10.1021/ja01877a043 . · doi:10.1021/ja01877a043
  3. Pew, J., & Weyna, P. (1962). Fine grinding, enzyme digestion and lignin-cellulose bond in wood. TAPPI, 45, 247–256.
  4. Mester, T., Varela, E., & Tien, M. (2004). Wood degradation by brown-rot and white-rot fungi. The Mycota II: genetics and biotechnology (2nd edition). Springer-Verlag Berlin-Heidelberg.
  5. Cai, D., & Tien, M. (1992). Kinetic studies on the formation and decomposition of compounds II and III. Journal of Biological Chemistry, 267, 1149–1155.
  6. Harvey, G.-F., Gilardi, G.-F., Goble, M. L., & Palmer, J. M. (1993). Charge transfer reactions and feedback control of lignin peroxidase by phenolic compounds: Significance in lignin degradation. Journal of Biotechnology, 30, 57–69, doi: 10.1016/0168-1656(93)90027-K . · doi:10.1016/0168-1656(93)90027-k
  7. Dodson, P. J., Evans, C. S., Harvey, P. J., & Palmer, J. M. (1987). Production and properties of an extracellular peroxidase from Corilus versicolor which catalyzes % MathType!Translator!2!1!AMS LaTeX.tdl!TeX -- AMS-LaTeX!% MathType!MTEF!2!1!+-% feaafiart1ev1aaatCvAUfeBSjuyZL2yd9gzLbvyNv2CaerbuLwBLn% hiov2DGi1BTfMBaeXatLxBI9gBaerbd9wDYLwzYbItLDharqqtubsr% 4rNCHbGeaGqiVu0Je9sqqrpepC0xbbL8F4rqqrFfpeea0xe9Lq-Jc9% vqaqpepm0xbba9pwe9Q8fs0-yqaqpepae9pg0FirpepeKkFr0xfr-x% fr-xb9adbaqaaeGaciGaaiaabeqaamaabaabaaGcbaGaae4qamaaBa% aaleaacqaHXoqyaeqaaOGaaeylaiaaboeadaWgaaWcbaGaeqOSdiga% beaaaaa!3BCB! $${\text{C}}_\alpha {\text{ - C}}_\beta $$ cleavage in a lignin model compound. FEMS Microbiology Letter, 42, 17–22.
  8. Chung, N., & Aust, S. D. (1995). Inactivation of lignin peroxidase by hydrogen peroxide during the oxidation of phenols. Archives of Biochemistry and Biophysics, 316, 851–855, doi: 10.1006/abbi.1995.1114 . · doi:10.1006/abbi.1995.1114
  9. Miki, K., Kondo, R., Renganathan, V., Mayfield, M. B., & Gold, M. H. (1988). Mechanism of aromatic ring cleavage of a β-biphenylyl ether dimer catalyzed by lignin peroxidase of Phanerochaete chrysosporium. Biochemistry, 27, 4787–4794, doi: 10.1021/bi00413a031 . · doi:10.1021/bi00413a031
  10. Umezawa, T., & Higuchi, T. (1989). Cleavages of aromatic ring and β-O-4 bond of synthetic lignin (DHP) by lignin peroxidase. FEB Letter, 242, 325–329, doi: 10.1016/0014-5793(89)80494-6 . · doi:10.1016/0014-5793(89)80494-6
  11. Schoemaker, H. E., & Leisola, M. S. A. (1990). Degradation of lignin by Phanerochaete chrysosporium. Journal of Biotechnology, 13, 101–109, doi: 10.1016/0168-1656(90)90096-T . · doi:10.1016/0168-1656(90)90096-t
  12. Khindaria, A., Grover, T. A., & Aust, S. D. (1995). Evidence for formation of the veratryl alcohol cation radical by lignin peroxidase. Biochemistry, 34, 6020–6025, doi: 10.1021/bi00018a003 . · doi:10.1021/bi00018a003
  13. Khindaria, A., Nie, G., & Aust, S. D. (1997). Detection and characterization of the lignin peroxidase compound II - veratryl alcohol cation radical complex. Biochemistry, 36, 14181–14185 doi: 10.1021/bi9715730 . · doi:10.1021/bi9715730
  14. Have, R. T., & Franssen, M. C. R. (2001). On a revised mechanism of side product formation in the lignin peroxidase catalyzed oxidation of veratryl alcohol. FEBS Letters, 487, 313–317 doi: 10.1016/S0014-5793(00)02379-6 . · doi:10.1016/s0014-5793(00)02379-6
  15. Baciocchi, E., Bietti, M., & Steenken, S. (1998). Lifetime, reduction potential and base-induced fragmentation of the veratryl alcohol radical cation in aqueous solution. Pulse radiolysis studies on a ligninase “mediator”. Journal of Physical Chemistry A, 102, 7337–7342, doi: 10.1021/jp9812482 . · DOI
  16. Joshi, D. K., & Gold, M. H. (1996). Oxidation of dimethoxylated aromatic compounds by lignin peroxidase from Phanerochaete chrysosporium. European Journal of Biochemistry, 237, 45–57, doi: 10.1111/j.1432-1033.1996.0045n.x . · doi:10.1111/j.1432-1033.1996.0045n.x
  17. Gettemy, J. M., Ma, B., Alic, M., & Gold, M. H. (1998). Reverse transcription-PCR analysis of the regulation of the manganese peroxidase gene family. Applied and Environmental Microbiology, 64, 569–574. · doi:10.1128/aem.64.2.569-574.1998
  18. Alic, M., Akileswaran, L., & Gold, M. H. (1997). Characterization of the gene encoding manganese peroxidase isozyme 3 from Phanerochaete chrysosporium. Biochimica et Biophysica Acta, 1338, 1–7. · doi:10.1016/s0167-4838(96)00235-x
  19. Mester, T., & Field, J. A. (1997). Optimization of manganese peroxidase production by the white rot fungus Bjerkandera sp. strain BOS55. FEMS Microbiology Letter, 155, 161–168, doi: 10.1111/j.1574-6968.1997.tb13873.x . · doi:10.1111/j.1574-6968.1997.tb13873.x
  20. Pease, E. A., & Tien, M. (1992). Heterogeneity and regulation of manganese peroxidases from Phanerochaete chrysosporium. Journal of Bacteriology, 174, 3532–3540. · doi:10.1128/jb.174.11.3532-3540.1992
  21. Kishi, K., Wariishi, H., Marquez, L., Dunford, H. B., & Gold, M. H. (1994). Mechanism of manganese peroxidase compound II reduction. Effect of organic acid chelators and pH. Biochemistry, 33, 8694–8701, doi: 10.1021/bi00195a010 . · doi:10.1021/bi00195a010
  22. Khindaria, A., Grover, T. A., & Aust, S. D. (1994). Oxalate-dependent reductive activity of manganese peroxidase from Phanerochaete chrysosporium. Archives of Biochemistry and Biophysics, 314, 301–306, doi: 10.1006/abbi.1994.1446 . · doi:10.1006/abbi.1994.1446
  23. Daina, S., Orlandi, M., Bestetti, G., Wiik, C., & Elegir, G. (2002). Degradation of β-5 lignin model dimers by Ceriporiopsis subvermispora. Enzyme Microbial Technology, 30, 499–505, doi: 10.1016/S0141-0229(01)00524-5 . · doi:10.1016/s0141-0229(01)00524-5
  24. Marco, A. E., & Roubelakis-Angelakis, K. A. (1997). Laccase activity could contribute to cell-wall reconstitution in regenerating protoplasts. Phytochemistry, 46, 421–425, doi: 10.1016/S0031-9422(97)00301-4 . · doi:10.1016/s0031-9422(97)00301-4
  25. Huang, H.-W., Zopellaro, G., & Sakurai, T. (1999). Spectroscopic and kinetic studies on the oxygen-centered radical formed during the four-electron reduction process of dioxygen by Rhus vernicifera laccase. Journal of Biological Chemistry, 274, 32718–32724, doi: 10.1074/jbc.274.46.32718 . · doi:10.1074/jbc.274.46.32718
  26. Zoppellaro, G., Huang, H.-W., & Sakurai, T. (2000). Kinetic studies on the reaction of the fully reduced laccase with dioxygen. Inorganic Reaction Mechanisms, 2, 79–84.
  27. Lundquist, K., & Kristersson, P. (1985). Exhaustive laccase-catalyzed oxidation of a lignin model compound (vanillyl glycol) produces methanol and polymeric quinoid products. Biochemistry Journal, 259, 277–279. · doi:10.1042/bj2290277
  28. Kamitsuji, H., Honda, Y., Watanabe, T., & Kuwahara, M. (2005). Mn2+ is dispensable for the production of active MnP2 by Pleurotus ostreatus. Biochemistry Biophysics Research Communication, 327, 871–876, doi: 10.1016/j.bbrc.2004.12.084 . · doi:10.1016/j.bbrc.2004.12.084

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Metadata

Authors
Wong, D. W. S.
Venue
Applied Biochemistry and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2008-06-26
Volume
157
Issue
2
Pages
174-209
ISSN
  • 0273-2289 (ISSN-L)
  • 1559-0291
DOI
10.1007/s12010-008-8279-z
OpenAlex
W2089687713
Cited by
892
References
183
FWCI
16.20
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)

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Wong, D. W. S. (2009). Structure and Action Mechanism of Ligninolytic Enzymes. Applied Biochemistry and Biotechnology. https://doi.org/10.1007/s12010-008-8279-z

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