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Spectroscopic and computational characterization of laccases and their substrate radical intermediates

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Abstract

Laccases are multicopper oxidases which oxidize a wide variety of aromatic compounds with the concomitant reduction of oxygen to water as by-product. Due to their high stability and biochemical versatility, laccases are key enzymes to be used as eco-friendly biocatalyst in biotechnological applications. The presence of copper paramagnetic species in the catalytic site paired with the substrate radical species produced in the catalytic cycle makes laccases particularly attractive to be studied by spectroscopic approaches. In this review, the potentiality of a combined multifrequency electron paramagnetic spectroscopy /computational approach to gain information on the nature of the catalytic site and radical species is presented. The knowledge at molecular level of the enzyme oxidative process can be of great help to model new enzymes with increased efficiency and robustness.

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Acknowledgments

This work was supported by the PRIN 2009-STNWX3 project of the Italian Ministry of Education, Universities and Research (MIUR) and by the Eco-Innovation European Project BISCOL (ECO/09/256112). Careful reading and revising of the manuscript by Les Brooks, Chemistry Professor Emeritus, Sonoma State University, is gratefully acknowledged.

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  1. Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy

    Rebecca Pogni, Maria Camilla Baratto, Adalgisa Sinicropi & Riccardo Basosi

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  1. Rebecca Pogni
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  2. Maria Camilla Baratto
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  4. Riccardo Basosi
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Correspondence to Riccardo Basosi.

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Pogni, R., Baratto, M.C., Sinicropi, A. et al. Spectroscopic and computational characterization of laccases and their substrate radical intermediates. Cell. Mol. Life Sci. 72, 885–896 (2015). https://doi.org/10.1007/s00018-014-1825-7

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