Pre-steady-state kinetic study on the formation of Compound I and II of ligninase
- 1 January 1989
- journal article
- research article
- Published by Elsevier BV in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 994 (1), 59-63
- https://doi.org/10.1016/0167-4838(89)90062-9
Abstract
No abstract availableKeywords
This publication has 12 references indexed in Scilit:
- The role of peroxidases, radical cations and oxygen in the degradation of ligninPhilosophical Transactions of the Royal Society of London. Series A, Mathematical and Physical Sciences, 1987
- Spectral characterization of the oxidized states of lignin peroxidase, an extracellular heme enzyme from the white rot basidiomycete Phanerochaete chrysosporiumBiochemistry, 1986
- Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporiumFEBS Letters, 1986
- Strategies for production of high ligninase activities by Phanerochaete chrysosporiumJournal of Biotechnology, 1985
- Aromatic ring cleavage of veratryl alcohol by Phanerochaete chrysosporiumFEBS Letters, 1985
- Single‐electron transfer processes and the reaction mechanism of enzymic degradation of ligninFEBS Letters, 1985
- On the mechanism of enzymatic lignin breakdownFEBS Letters, 1985
- Studies on Horseradish PeroxidasePublished by Elsevier BV ,1972
- pH Dependence of the oxidation of iodide by compound I of horseradish peroxidaseBiochemistry, 1972