Abstract
The ability of white rot fungi to degrade a wide variety of environmental pollutants and the possibility of use of this technology for bioremediation has led to considerable research effort in academic, industrial and governmental agencies. This review discusses the advantages that these fungi possess over other bioremediation agents from a mechanistic standpoint.
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References
Sarkanen, K.V. and Ludwig, C.H. (1971) in Lignins: Occurrence, Formation and Structure, Wiley-Interscience, New York, pp. 1–18.
Tien, M. and Kirk, T.K. (1984) Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H2O2-requiring oxygenase, Proc. Natl. Acad. Sci. USA 81, 2280–2284.
Gold, M.H., Kuwahara, M., Chiu, A.A., and Glenn, J.K. (1984) Purification and characterization of an extracellular H2O2-requiring diarylpropane oxygenase from the lignin-degrading basidiomycete, Phanerochaete chrysosporium, Arch. Biochem. Biophys. 234, 353362.
Lundquist, K. and Kirk, T.K. (1978) De Novo synthesis and decomposition of veratryl alchol by a lignin-degrading basidiomycetes, Phytochemistry 17, 1676.
Kuan, I.C. and Tien, M. (1993) Proc. Natl. Acad. Sci. USA 90, 1242–1246.
Tien, M. (1987) Properties of ligninase from Phanerochaete chrysosporiumand their possible applications, CRC Crit. Rev. Microbiol. 15, 141–168.
Dunford, H.B. (1982) Adv. Inorg. Biochem. 4, 41–68.
Khindaria, A. and Aust, S.D. (1996) EPR detection and characterization of lignin peroxidase porphyrin π cation radical, Biochemistry (Submitted).
Schulz, C.E., Devaney, P.W., Winkler, H., Debrunner, P.G., Doan, N., Chiang, R., Rutter, R., and Hager, L.P. (1979) Horseradish peroxidase compound I: Evidence for spin coupling between the heme iron and a “free radical”, FEBS Lett. 103, 102–105.
Glenn, J.K. and Gold, M.H. (1985) Purification and characterization of an extracellular Mn(II)-dependent peroxidase from lignin-degradation Basidiomyete, Arch. Biochem. Biophys. 242, 329–341.
Tien, M., Kirk, T.K., Bull, C., and Fee, J.A. (1986) Steady-state and transient-state kinetic studies on the oxidation of 3,4dimethoxybenzyl alcohol catalyzed by the ligninase of Phanerochaete chrysosporium Burds, J. Biol. Chem. 261, 1687 1693.
Khindaria, A., Grover, T.A., and Aust, S.D. (1995) Evidence for formation of the veratryl alcohol cation radical by lignin peroxidase, Biochemistry 34, 6020–6025.
Khindaria, A., Yamazaki, I., and S.D. Aust (1995) Veratryl alcohol oxidation by lignin peroxidase, Biochemistry 34, 16860–16869.
Khindaria, A., Yamazaki, I., and Aust, S.D. (1996) Stabilization of the veratryl alcohol cation radical by lignin peroxidase, Biochemistry 35, 6418–6424.
Poulos, T.L., Edwards, S.L., Wariishi, H., and Gold, M.H. (1993) Crystallographic refinement of lignin peroxidase at 2Â, J. Biol. Chem. 268, 4429–4440.
Khindaria, A. and Aust, S.D. (1996) EPR detection and characterization of lignin peroxidase compound II-veratryl alcohol cation radical. (In preparation).
Hoffman, B.M., Roberts, J.E., Kang, C.H., and Margoliash, E. (1981) Electron paramagnetic and eletron nuclear double resonance of hydrogen peroxide compound of cytochrome c peroxidase, Biochemistry 256, 6556–6564.
Goodwin, D.C., Aust, S.D., and Grover, T.A. (1995) Evidence for veratryl alcohol as a redox mediator in lignin peroxidase-catalyzed oxidation, Biochemistry 34, 5060–5065.
Chung, N. and Aust, S.D. (1995) Veratryl alcohol-mediated indirect oxidation of phenol by lignin peroxidase, Arch. Biochem. Biophys. 316, 733–737.
Hammel, K.E., Tien, M., Kalyanaraman, B., and Kirk, T.K. (1985) Mechanism of oxidative Ca-Cß cleavage of a lignin model dimer by Phanerochaete chrysosporium ligninase, J Biol. Chem. 260, 8348–8353.
Shah, M.M., Grover, T.A., Barr, D.P., and Aust, S.D. (1992) On the mechanism of inhibition of the veratryl alcohol oxidase activity of lignin peroxidase H2 by EDTA, J Biol. Chem. 267, 21564–21569.
Shah, M.M., Grover, T.A., and Aust, S.D. (1993) Reduction of CCI4 to the trichloromethyl radical by lignin peroxidase H2 from Phanerochaete chrysosporium, Biochem. Biophys. Res. Comms. 191, 887–892.
Khindaria, A., Grover, T.A., and Aust, S.D. (1995) Reductive dehalogenation of aliphatic halocarbons by lignin peroxidase of Phanerochaete chrysosporium, Environ. Sci. Technol. 29, 719–725.
Khindaria, A., Grover, T.A., and Aust, S.D. (1994) Oxalate dependent reductive activity of manganese peroxidase from Phanerochaete chrysosporium, Arch. Biochem. Biophys. 314, 301–306.
Rasmussen, S.J., Chung, N., Khindaria, A., Grover, T.A., and Aust, S.D. (1995) Reductions catalyzed by a quinone and peroxidases from Phanerochaete chrysosporium, Arch. Biochem. Biophys. 320, 243–249.
Stahl, J.D., Rasmussen, S.J., and Aust, S.D. (1995) Reduction of quinones and radicals by a plasma membrane redox system of Phanerochaete chrysosporium, Arch. Biochem. Biophys. 322, 221–227.
Barr, D.P., Shah, M.M., Grover, T.A., and Aust, S.D. (1992) Production of hydroxyl radical by lignin peroxidase from Phanerochaete chrysosporium, Arch. Biochem. Biophys. 298, 480–485.
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Khindaria, A., Aust, S.D. (1997). Free Radical Reactions Catalyzed by Peroxidases from White Rot Fungi. In: Minisci, F. (eds) Free Radicals in Biology and Environment. NATO ASI Series, vol 27. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-1607-9_32
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DOI: https://doi.org/10.1007/978-94-017-1607-9_32
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