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Catalytic Efficiency of Basidiomycete Laccases: Redox Potential versus Substrate-Binding Pocket Structure

A. N. Bach Institute of Biochemistry, Research Center of Biotechnology, Russian Academy of Sciences, Leninsky Ave. 33/2, 119071 Moscow, Russia
Faculty of Bioengineering and Bioinformatics, Moscow State University, 119992 Moscow, Russia
All-Russian Research Institute for Optophysical Measurements (VNIIOFI), Ozernaya 46, 119361 Moscow, Russia
Author to whom correspondence should be addressed.
Catalysts 2018, 8(4), 152;
Received: 15 March 2018 / Revised: 30 March 2018 / Accepted: 2 April 2018 / Published: 9 April 2018
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Laccases are copper-containing oxidases that catalyze a one-electron abstraction from various phenolic and non-phenolic compounds with concomitant reduction of molecular oxygen to water. It is well-known that laccases from various sources have different substrate specificities, but it is not completely clear what exactly provides these differences. The purpose of this work was to study the features of the substrate specificity of four laccases from basidiomycete fungi Trametes hirsuta, Coriolopsis caperata, Antrodiella faginea, and Steccherinum murashkinskyi, which have different redox potentials of the T1 copper center and a different structure of substrate-binding pockets. Enzyme activity toward 20 monophenolic substances and 4 phenolic dyes was measured spectrophotometrically. The kinetic parameters of oxidation of four lignans and lignan-like substrates were determined by monitoring of the oxygen consumption. For the oxidation of the high redox potential (>700 mV) monophenolic substrates and almost all large substrates, such as phenolic dyes and lignans, the redox potential difference between the enzyme and the substrate (ΔE) played the defining role. For the low redox potential monophenolic substrates, ΔE did not directly influence the laccase activity. Also, in the special cases, the structure of the large substrates, such as dyes and lignans, as well as some structural features of the laccases (flexibility of the substrate-binding pocket loops and some amino acid residues in the key positions) affected the resulting catalytic efficiency. View Full-Text
Keywords: laccase; substrate specificity; redox potential; substrate-binding-pocket; dilignan laccase; substrate specificity; redox potential; substrate-binding-pocket; dilignan

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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).

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Glazunova, O.A.; Trushkin, N.A.; Moiseenko, K.V.; Filimonov, I.S.; Fedorova, T.V. Catalytic Efficiency of Basidiomycete Laccases: Redox Potential versus Substrate-Binding Pocket Structure. Catalysts 2018, 8, 152.

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