Crystal structure of an ascomycete fungal laccase from <i>Thielavia arenaria</i> – common structural features of asco‐laccases

Kallio, J.P.; Gasparetti, Chiara; Andberg, Martina; Boer, Harry; Koivula, Anu; Kruus, Kristiina; Rouvinen, Juha; Hakulinen, Nina

doi:10.1111/j.1742-4658.2011.08146.x

Cited by 76 publications

(61 citation statements)

References 64 publications

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“…Above 35°C, the currents decrease and signal distortion occurs due to protein desorption and/or unfolding. The E°' values for McoG wt and variants are similar to those reported for the T1 center of low potential laccases immobilized within an electrochemically inert polymer coating a gold electrode surface [35] and to those of other asco-laccases [36].…”

Section: Electrochemical Propertiessupporting

confidence: 79%

“…The crystal structure obtained from crystal form II consists of 549 amino acid residues (the first 21 amino acid residues are not visible), four copper ions, fourteen glucosides, one peroxide molecule and 599 solvent molecules. The two models are very similar and their overall structure is similar to that of other laccases, especially to those from the ascomycetes Melanocarpus albomyces (MaL) [36] and Thielavia arenaria (TaL) ( Figure 4A) [42]. The least square superposition of the Cα atoms of the McoG structure (crystal form I) with those of MaL and TaL gave an rmsd of 1.41 and 1.48 Å, respectively.…”

Section: Structural Propertiesmentioning

confidence: 70%

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Structure and function of Aspergillus niger laccase McoG

Ferraroni¹,

Westphal²,

Borsani³

et al. 2017

Biocatalysis

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Biocatalysis 2017; 3: 1-16 p-phenylenediamine sulphate. However, the activities of H253A and H253N with 2-amino-4-methylphenol and 2-amino-4-methoxyphenol are strongly reduced compared to that of wild type. The redox potentials and electron transfer rates (k s ) of wild type and variants were determined (McoG wt E°' is +453 mV), and especially the reduced k s values of H253A and H253N show strong correlation with their low activity on phenolic compounds. In summary, our results suggest that the His253 adaptation of McoG can be beneficial for the conversion of phenolic compounds.Keywords: Aspergillus niger; crystal structure; laccase; redox potential; metalloprotein; multicopper oxidase Data deposition: Coordinates have been deposited with the Protein Data Bank. Accession codes are 5LM8, 5LWW and 5LWX.Abbreviations: CV, cyclic voltammetry; DT, decane-1-thiol; MCO, multicopper oxidase; MaL, laccase from Melanocarpus albomyces; TaL, laccase from Thielavia arenaria; SAM, self-assembled monolayer; SCE, saturated calomel electrode; SHE, standard hydrogen electrode; DMPPDA, N,N-dimethyl-p-phenylenediamine; ABTS, 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulphonic acid). IntroductionMulticopper oxidases (MCOs) form a family of redox enzymes that catalyze the reduction of molecular oxygen into water by a four-electron transfer process. It includes laccases (EC 1.10.3.2), ascorbate oxidases (EC 1.10.3.3), bilirubin oxidases (EC 1.3.3.5) and ferroxidases (EC 1.16.3.1), which are key enzymes in many biological processes of prokaryotic and eukaryotic organisms [1,2]. Their ability to catalyze the oxidation of various aromatic substrates with the concomitant reduction of molecular oxygen to water as sole byproduct makes them interesting green biocatalysts. The MCO catalyzed redox process is mediated by two copper centers, which contain Abstract: The ascomycete Aspergillus niger produces several multicopper oxidases, but their biocatalytic properties remain largely unknown. Elucidation of the crystal structure of A. niger laccase McoG at 1.7 Å resolution revealed that the C-terminal tail of this glycoprotein blocks the T3 solvent channel and that a peroxide ion bridges the two T3 copper atoms. Remarkably, McoG contains a histidine (His253) instead of the common aspartate or glutamate expected to be involved in catalytic proton transfer with phenolic compounds. The crystal structure of H253D at 1.5 Å resolution resembles the wild type structure. McoG and the H253D, H253A and H253N variants have similar activities with 2,2'-azino-bis (3-ethylbenzothiazoline-6-sulphonic acid or N,N-dimethyl-

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Section: Electrochemical Propertiessupporting

confidence: 79%

Section: Structural Propertiesmentioning

confidence: 70%

Structure and function of Aspergillus niger laccase McoG

Ferraroni¹,

Westphal²,

Borsani³

et al. 2017

Biocatalysis

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“…The kinetic data of TaLcc1 thus should fit in between those of the two enzymes. However, data on kinetic parameters of this enzyme (38) showed this not to be the case, suggesting that the redox potential difference between the T1 copper and the substrate may not be the only factor that contributes to substrate oxidation. It has also been reported that a variant of the Pleurotus ostreatus laccase (1H6C) which showed a higher redox potential (by ϩ0.12 V) relative to the wild-type enzyme exhibited catalytic efficiencies similar to those of the wild type on several substrates (39).…”

Section: Discussionmentioning

confidence: 95%

Structural Insights into 2,2′-Azino-Bis(3-Ethylbenzothiazoline-6-Sulfonic Acid) (ABTS)-Mediated Degradation of Reactive Blue 21 by Engineered Cyathus bulleri Laccase and Characterization of Degradation Products

Kenzom

Srivastava

Mishra

2014

Appl Environ Microbiol

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Advanced oxidation processes are currently used for the treatment of different reactive dyes which involve use of toxic catalysts. Peroxidases are reported to be effective on such dyes and require hydrogen peroxide and/or metal ions. Cyathus bulleri laccase, expressed in Pichia pastoris, catalyzes efficient degradation (78 to 85%) of reactive azo dyes (reactive black 5, reactive orange 16, and reactive red 198) in the presence of synthetic mediator ABTS [2,2=-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid)]. This laccase was engineered to degrade effectively reactive blue 21 (RB21), a phthalocyanine dye reported to be decolorized only by peroxidases. The 816-bp segment (toward the C terminus) of the lcc gene was subjected to random mutagenesis and enzyme variants (Lcc35, Lcc61, and Lcc62) were selected based on increased ABTS oxidizing ability. Around 78 to 95% decolorization of RB21 was observed with the ABTS-supplemented Lcc variants in 30 min. Analysis of the degradation products by mass spectrometry indicated the formation of several low-molecular-weight compounds. Mapping the mutations on the modeled structure implicated residues both near and far from the T1 Cu site that affected the catalytic efficiency of the mutant enzymes on ABTS and, in turn, the rate of oxidation of RB21. Several inactive clones were also mapped. The importance of geometry as well as electronic changes on the reactivity of laccases was indicated.

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“…Some extremophilic fungi like Penicillium pinophilum isolated from Himalayan region was demonstrated to produce laccase at low temperatures [104]. However the mechanism of action of laccases under extreme conditions is less explored, with crystal structure of only a few laccases being fully known including those from ascomycetes Melanocarpus albomyces (MaL) and Thielavia arenaria (TaLcc1) which differ from other laccases by the presence of a conserved 'C-terminal plug' probably in proton transfer processes [105]. In spite of their tremendous potential in bioremediation, the utility of laccases is restricted by their low shelf life.…”

Section: Laccasementioning

confidence: 99%

Diverse Metabolic Capacities of Fungi for Bioremediation

2016

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Bioremediation refers to cost-effective and environment-friendly method for converting the toxic, recalcitrant pollutants into environmentally benign products through the action of various biological treatments. Fungi play a major role in bioremediation owing to their robust morphology and diverse metabolic capacity. The review focuses on different fungal groups from a variety of habitats with their role in bioremediation of different toxic and recalcitrant compounds; persistent organic pollutants, textile dyes, effluents from textile, bleached kraft pulp, leather tanning industries, petroleum, polyaromatic hydrocarbons, pharmaceuticals and personal care products, and pesticides. Bioremediation of toxic organics by fungi is the most sustainable and green route for cleanup of contaminated sites and we discuss the multiple modes employed by fungi for detoxification of different toxic and recalcitrant compounds including prominent fungal enzymes viz., catalases, laccases, peroxidases and cyrochrome P450 monooxygeneses. We have also discussed the recent advances in enzyme engineering and genomics and research being carried out to trace the less understood bioremediation pathways.

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Crystal structure of an ascomycete fungal laccase from Thielavia arenaria – common structural features of asco‐laccases

Cited by 76 publications

References 64 publications

Structure and function of Aspergillus niger laccase McoG

Structure and function of Aspergillus niger laccase McoG

Structural Insights into 2,2′-Azino-Bis(3-Ethylbenzothiazoline-6-Sulfonic Acid) (ABTS)-Mediated Degradation of Reactive Blue 21 by Engineered Cyathus bulleri Laccase and Characterization of Degradation Products

Diverse Metabolic Capacities of Fungi for Bioremediation

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