Lignin peroxidase of Phanerochaete chrysosporium. Evidence for an acidic ionization controlling activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Spectral characterization of diarylpropane oxygenase, a novel peroxide-dependent, lignin-degrading heme enzyme.
2. Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium.
3. Characterization of two lignin peroxidase clones from Phanerochaete chrysosporium
4. Horseradish peroxidase. XLI. Complex formation with nitrate and its effect upon compound I formation
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1. Oxidation of polyaromatic hydrocarbons in systems containing water miscible organic solvents by the lignin peroxidase ofGleophyllum striatumMTCC‐1117;Environmental Technology;2011-08
2. Combined treatment of textile effluent using the sequence Phanerochaete chrysosporium–ozone;Chemosphere;2001-07
3. Kinetic evidence for surface residues influencing the active site of Coprinus cinereus peroxidase: analysis of the pH dependence of G154E, P90H and P90H–G154E substrate entrance mutants;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2001-01
4. Purification and characterization of two lignin peroxidase isozymes produced byBjerkanderasp. strain BOS55;FEBS Letters;1998-02-06
5. Cloning and Biochemical Characterization of an Anionic Peroxidase from Zea Mays;European Journal of Biochemistry;1997-08
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