Three-dimensional structure of laccase from Coriolus zonatus at 2.6 Å resolution

Lyashenko, A. V.; Zhukova, Yu. N.; Жухлистова, Н. Е.; Zaĭtsev, V. N.; Степанова, Елена В.; Качалова, Г.С.; Королева, О. В.; Voelter, Wolfgang; Betzel, C.; Tishkov, V. I.; Bento, Isabel; Габдулхаков, А.Г.; Morgunova, Ekaterina; Lindley, P. F.; Mikhailov, A.M.

doi:10.1134/s1063774506050117

Cited by 14 publications

(8 citation statements)

References 18 publications

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“…Second-derivative IR spectra demonstrate a partial substitution of bound water molecules by ethanol molecules in terms of upward shifts of CO stretch frequencies due to weaker H-bonds (Figure S7). Particularly, band positions (1800–1700 cm –1 ) related to CO stretch in aspartate and glutamate residues constituting the solvent channel to T2 copper , have all shifted 2–3 cm –1 up, indicating that its inner hydrophilic “wall” was decorated with ethanol molecules. Transport of hydrophobic oxygen molecules to the reduction site might be facilitated through the ethanol-substituted solvent channel, which merits our in-depth research attention.…”

Section: Resultsmentioning

confidence: 99%

Role of Organic Solvents in Immobilizing Fungus Laccase on Single-Walled Carbon Nanotubes for Improved Current Response in Direct Bioelectrocatalysis

et al. 2017

J. Am. Chem. Soc.

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Improving bioelectrocatalytic current response of redox enzymes on electrodes has been a focus in the development of enzymatic biosensors and biofuel cells. Herein a mediatorless electroreduction of oxygen is effectively improved in terms of a remarkable enhancement by ca. 600% in maximum reductive current by simply adding 20% ethanol into laccase solution during its immobilization onto single-walled carbon nanotubes (SWCNTs). Conformation analysis by circular dichroism and attenuated total reflectance infrared spectroscopy demonstrate promoted laccase-SWCNTs contact by ethanol, thus leading to favorable enzyme orientation on SWCNTs. Extended investigation on acetone-, acetonitrile-, N,N-dimethylformamide (DMF)-, or dimethyl sulfoxide (DMSO)-treated laccase-SWCNTs electrodes shows a 400% and 350% current enhancement at maxima upon acetone and acetonitrile treatment, respectively, and a complete diminish of reductive current by DMF and DMSO. These results together reveal the important role of organic solvents in regulating laccase immobilization for direct bioelectrocatalysis by balancing surface wetting and protein denaturing.

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Section: Resultsmentioning

confidence: 99%

Role of Organic Solvents in Immobilizing Fungus Laccase on Single-Walled Carbon Nanotubes for Improved Current Response in Direct Bioelectrocatalysis

et al. 2017

J. Am. Chem. Soc.

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“…Laccases are known to bind four copper(II) ions in three different binding sites, each characterized by unique spectroscopic properties and playing an important role in substrate oxidation. ,− The paramagnetic type 1 (T1) copper is coordinated by two His residues, one Met residue, and one Cys residue. The tight coordination of T1 copper to the Cys residue is responsible for an intense absorption band around 600 nm, giving the blue color to the enzyme.…”

Section: Resultsmentioning

confidence: 99%

“…The T3 coppers are antiferromagnetically coupled with the EPR silent pair absorption maximum at 330 nm. The one T2 copper and two T3 coppers are arranged in a trinuclear cluster, which is believed to be the site of molecular oxygen reduction. , The catalytic cycle is thought to be initiated by oxidation of the substrate near the T1 copper site by transfer of an electron from the substrate. In total, four electrons (produced by oxidation of four substrates) are then sequentially transferred from the T1 copper to the trinuclear cluster along a Cys-His pathway, where one oxygen molecule is reduced to two water molecules to complete the cycle …”

Section: Resultsmentioning

confidence: 99%

Roles of Small Laccases fromStreptomycesin Lignin Degradation

et al. 2014

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Laccases (EC 1.10.3.2) are multicopper oxidases that can oxidize a range of substrates, including phenols, aromatic amines, and nonphenolic substrates. To investigate the involvement of the small Streptomyces laccases in lignin degradation, we generated acid-precipitable polymeric lignin obtained in the presence of wild-type Streptomyces coelicolor A3(2) (SCWT) and its laccase-less mutant (SCΔLAC) in the presence of Miscanthus x giganteus lignocellulose. The results showed that strain SCΔLAC was inefficient in degrading lignin compared to strain SCWT, thereby supporting the importance of laccase for lignin degradation by S. coelicolor A3(2). We also studied the lignin degradation activity of laccases from S. coelicolor A3(2), Streptomyces lividans TK24, Streptomyces viridosporus T7A, and Amycolatopsis sp. 75iv2 using both lignin model compounds and ethanosolv lignin. All four laccases degraded a phenolic model compound (LM-OH) but were able to oxidize a nonphenolic model compound only in the presence of redox mediators. Their activities are highest at pH 8.0 with a low krel/Kapp for LM-OH, suggesting that the enzymes’ natural substrates must be different in shape or chemical nature. Crystal structures of the laccases from S. viridosporus T7A (SVLAC) and Amycolatopsis sp. 75iv2 were determined both with and without bound substrate. This is the first report of a crystal structure for any laccase bound to a nonphenolic β-O-4 lignin model compound. An additional zinc metal binding site in SVLAC was also identified. The ability to oxidize and/or rearrange ethanosolv lignin provides further evidence of the utility of laccase activity for lignin degradation and/or modification.

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“…The first complete laccase structures were published in 2002, and crystal structures from at least 10 different organisms have now been reported. Most of the structures are from sporophoral basidiomycota fungi: Coprinus cinereus [10], Trametes versicolor [11,12], Rigidoporus lignosus [13], Cerrena maxima [14], Coriolus zonatus [15], Lentinus tigrinus [16], Trameter trogii [17], Trametes hirsuta [18], and Coriolopsis gallica . Structures of bacterial laccases or multicopper oxidases are also available, including the spore coat protein A from Bacillus subtilis [20], a copper efflux operob from E. coli [21], and the more recently published novel two‐domain laccases [22–24].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2011

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Laccases are copper‐containing enzymes used in various applications, such as textile bleaching. Several crystal structures of laccases from fungi and bacteria are available, but ascomycete types of fungal laccases (asco‐laccases) have been rather unexplored, and to date only the crystal structure of Melanocarpus albomyces laccase (MaL) has been published. We have now solved the crystal structure of another asco‐laccase, from Thielavia arenaria (TaLcc1), at 2.5 Å resolution. The loops near the T1 copper, forming the substrate‐binding pockets of the two asco‐laccases, differ to some extent, and include the amino acid thought to be responsible for catalytic proton transfer, which is Asp in TaLcc1, and Glu in MaL. In addition, the crystal structure of TaLcc1 does not have a chloride attached to the T2 copper, as observed in the crystal structure of MaL. The unique feature of TaLcc1 and MaL as compared with other laccases structures is that, in both structures, the processed C‐terminus blocks the T3 solvent channel leading towards the trinuclear centre, suggesting a common functional role for this conserved ‘C‐terminal plug’. We propose that the asco‐laccases utilize the C‐terminal carboxylic group in proton transfer processes, as has been suggested for Glu498 in the CotA laccase from Bacillus subtilis. The crystal structure of TaLcc1 also shows the formation of a similar weak homodimer, as observed for MaL, that may determine the properties of these asco‐laccases at high protein concentrations. Database  Structural data are available in the Protein Data Bank database under the accession numbers http://www.rcsb.org/pdb/search/structidSearch.do?structureId=3PPS and http://www.rcsb.org/pdb/search/structidSearch.do?structureId=2VDZ Structured digital abstract http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=nucleotide&cmd=Retrieve&dopt=Graphics&list_uids=$ http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0407 to http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=nucleotide&cmd=Retrieve&dopt=Graphics&list_uids=$ by http://www.ebi.ac.uk/ontology-lookup/?termId=MI:0114 http://mint.bio.uniroma2.it/mint/search/interaction.do?interactionAc=MINT-8173385

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Three-dimensional structure of laccase from Coriolus zonatus at 2.6 Å resolution

Cited by 14 publications

References 18 publications

Role of Organic Solvents in Immobilizing Fungus Laccase on Single-Walled Carbon Nanotubes for Improved Current Response in Direct Bioelectrocatalysis

Role of Organic Solvents in Immobilizing Fungus Laccase on Single-Walled Carbon Nanotubes for Improved Current Response in Direct Bioelectrocatalysis

Roles of Small Laccases fromStreptomycesin Lignin Degradation

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

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