title: Spectroscopic and computational characterization of laccases and their substrate radical intermediates.
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.
authors.affiliation: Department of Biotechnology, Chemistry and Pharmacy, University of Siena, Via A Moro 2, 53100, Siena, Italy.
authors.forename: Rebecca
authors.initials: R
authors.lastname: Pogni
authors.forename: Maria Camilla
authors.initials: MC
authors.lastname: Baratto
authors.forename: Adalgisa
authors.initials: A
authors.lastname: Sinicropi
authors.forename: Riccardo
authors.initials: R
authors.lastname: Basosi
mesh_terms: D001463:Barbiturates / Q000737:chemistry; D055162:Biocatalysis; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D004578:Electron Spin Resonance Spectroscopy; D042845:Laccase / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D001463:Barbiturates; C094277:violuric acid; D003300:Copper; D042845:Laccase