Crystal Structure of a Laccase from the FungusTrametes versicolor at 1.90-Å Resolution Containing a Full Complement of Coppers*
By K. Piontek, M. Antorini, T. Choinowski. Journal of Biological Chemistry, 2002
843 citations recorded by the source corpus.
Laccase is a polyphenol oxidase, which belongs to the family of blue multicopper oxidases. These enzymes catalyze the one-electron oxidation of four reducing-substrate molecules concomitant with the four-electron reduction of molecular oxygen to water. Laccases oxidize a broad range of substrates, preferably phenolic compounds. In the presence of mediators, fungal laccases exhibit an enlarged substrate range and are then able to oxidize compounds with a redox potential exceeding their own. Until now, only one crystal structure of a laccase in an inactive, type-2 copper-depleted form has been reported. We present here the first crystal structure of an active laccase containing a full complement of coppers, the complete polypeptide chain together with seven carbohydrate moieties. Despite the presence of all coppers in the new structure, the folds of the two laccases are quite similar. The coordination of the type-3 coppers, however, is distinctly different. The geometry of the trinuclear copper cluster in the Trametes versicolor laccase is similar to that found in the ascorbate oxidase and that of mammalian ceruloplasmin structures, suggesting a common reaction mechanism for the copper oxidation and the O2 reduction. In contrast to most blue copper proteins, the type-1 copper in the T. versicolorlaccase has no axial ligand and is only 3-fold coordinated. Previously, a modest elevation of the redox potential was attributed to the lack of an axial ligand. Based on the present structural data and sequence comparisons, a mechanism is presented to explain how laccases could tune their redox potential by as much as 200 mV.
Subfields: Biotechnology, Cell Biology, Plant Science
View Paper: https://www.semanticscholar.org/paper/1125639bd77bde9ed70531306ab187b17980ebf2
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Citations in the corpus
- Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin. (2005, background): “The molecular environment of laccase type-I copper seems to regulate the redox potential of the enzyme [37].”
- Lignin Biodegradation with Laccase-Mediator Systems (2014, background): “Type 2 copper coordinates with two histidines and a water molecule; it is colorless with no absorption in the visible spectrum (Piontek et al., 2002).”
- Structure and Action Mechanism of Ligninolytic Enzymes (2009, background): “vernicifera enzyme has a value of 420 mV [154, 159, 162].”
- Effect of different seeding methods on green manure biomass, soil properties and rice yield in rice-based cropping systems (2011, background): “2; benzenediol: oxygen oxidoreductase) are a family of multicopper oxidases that require O2 to oxidize organic compounds, particularly phenols (Piontek et al., 2002) and different non-phenolic substrates by one-electron transfer, resulting in the formation of reactive radicals, while reducing molecu”
- Laccases: a never-ending story (2010, background): “Piontek and coworkers [23] have hypothesized a correlation between the coordination distances around the Cu1 ion and its E: the longer the distance the higher is E.”
- Biological pretreatment of lignocelluloses with white-rot fungi and its applications: A review (2011, background): “The complete crystalline structure of laccase containing all four copper atoms in the active site has been published from T. versicolor and Cerrena maxima (Bertrand et al. 2002; Piontek et al. 2002).”