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 mechanism
- 1 January 2001
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 305 (4), 851-861
- https://doi.org/10.1006/jmbi.2000.4346
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- 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
- Spectral Changes of Lignin Peroxidase during Reversible InactivationBiochemistry, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- SETOR: Hardware-lighted three-dimensional solid model representations of macromoleculesJournal of Molecular Graphics, 1993
- Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 Å resolutionFEBS Letters, 1993
- Characterization of a highly expressed lignin peroxidase-encoding gene from the basidiomycete Phanerochaete chrysosporiumGene, 1992
- Kinetics and energetics of one-electron-transfer reactions involving tryptophan neutral and cation radicalsThe Journal of Physical Chemistry, 1991
- CHAIN — A crystallographic modeling programJournal of Molecular Graphics, 1988
- Analysis of nucleotide sequences of two ligninase cDNAs from a white-rot filamentous fungus, Phanerochaete chrysosporiumGene, 1987
- Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporiumFEBS Letters, 1986