caa a22 4500 606176861 CHVBK 20210128100749.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00018-014-1825-7 doi (NATIONALLICENCE)springer-10.1007/s00018-014-1825-7 Spectroscopic and computational characterization of laccases and their substrate radical intermediates [Elektronische Daten] [Rebecca Pogni, Maria Baratto, Adalgisa Sinicropi, Riccardo Basosi] 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. Springer Basel, 2015 Multicopper oxidases nationallicence Copper catalytic site nationallicence Laccase's catalytic mechanism nationallicence Substrate oxidation nationallicence Paramagnetic species nationallicence Radical intermediates nationallicence EPR spectroscopy nationallicence DFT calculations nationallicence Pogni Rebecca Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut Baratto Maria Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut Sinicropi Adalgisa Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut Basosi Riccardo Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut Cellular and Molecular Life Sciences Springer Basel 72/5(2015-03-01), 885-896 1420-682X 72:5<885 2015 72 18 https://doi.org/10.1007/s00018-014-1825-7 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-014-1825-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Pogni Rebecca Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut NATIONALLICENCE 700 1- Baratto Maria Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut NATIONALLICENCE 700 1- Sinicropi Adalgisa Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut NATIONALLICENCE 700 1- Basosi Riccardo Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/5(2015-03-01), 885-896 1420-682X 72:5<885 2015 72 18