Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in β‐O‐4 linkage
- 4 March 2004
- journal article
- Published by Wiley in FEBS Letters
- Vol. 562 (1-3) , 197-201
- https://doi.org/10.1016/s0014-5793(04)00224-8
Abstract
An investigation was performed to determine whether lignin dehydrogenative polymerization proceeds via radical mediation or direct oxidation by peroxidases. It was found that coniferyl alcohol radical transferred quickly to sinapyl alcohol. The transfer to syringaresinol was slower, however, the transfer to polymeric lignols occurred very slightly. This result suggests that the radical mediator theory does not sufficiently explain the mechanism for dehydrogenative polymerization of lignin. A cationic cell wall peroxidase (CWPO-C) from poplar (Populus alba L.) callus showed a strong substrate preference for sinapyl alcohol and the sinapyl alcohol dimer, syringaresinol. Moreover, CWPO-C was capable of oxidizing high-molecular-weight sinapyl alcohol polymers and ferrocytochrome c. Therefore, the CWPO-C characteristics are important to produce polymer lignin. The results suggest that CWPO-C may be a peroxidase isoenzyme responsible for the lignification of plant cell walls.Keywords
This publication has 20 references indexed in Scilit:
- Treatment of poplar callus with ferulic and sinapic acids I: incorporation and enhancement of lignin biosynthesisJournal of Wood Science, 2003
- Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanismJournal of Molecular Biology, 2001
- Regioselectivity in lignin biosynthesis. The influence of dimerization and cross-couplingJournal of the Chemical Society, Perkin Transactions 1, 2000
- The crystal structure of lignin peroxidase at 1.70 Å resolution reveals a hydroxy group on the C β of tryptophan 171: A novel radical site formed during the redox cycle 1 1Edited by R. HuberJournal of Molecular Biology, 1999
- Substrate-Specific Peroxidases in Woody Angiosperms and Gymnosperms Participate in Regulating the Dehydrogenative Polymerization of Syringyl and Guaiacyl Type LigninsHolzforschung, 1998
- Oxidative cross coupling of p-hydroxycinnamic alcohols with dimeric arylglycerol β-aryl ether lignin model compounds. The effect of oxidation potentialsJournal of the Chemical Society, Perkin Transactions 1, 1998
- Oxidation of hydroxycinnamic acid and hydroxycinnamyl alcohol derivatives by laccase and peroxidase. Interactions among p‐hydroxyphenyl, guaiacyl and syringyl groups during the oxidation reactionsPhysiologia Plantarum, 1995
- Oxidation of Ferrocytochrome c by Lignin PeroxidaseBiochemistry, 1994
- Facile large-scale synthesis of coniferyl, sinapyl, and p-coumaryl alcoholJournal of Agricultural and Food Chemistry, 1992