Please use this identifier to cite or link to this item: http://hdl.handle.net/20.500.12779/6523
Title: Spectroscopic and computational characterization of laccases and their substrate radical intermediates.
Authors: Pogni, Rebecca 
Baratto, Maria Camilla 
Sinicropi, Adalgisa 
Basosi, Riccardo 
Keywords: Copper catalytic site; DFT calculations; EPR spectroscopy; Laccase’s catalytic mechanism; Multicopper oxidases; Paramagnetic species; Radical intermediates; Substrate oxidation
Issue Date: 2015
Project: None 
Journal: CELLULAR AND MOLECULAR LIFE SCIENCES
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
Description: 
76450
URI: http://hdl.handle.net/20.500.12779/6523
ISSN: 1420-9071
DOI: 10.1007/s00018-014-1825-7
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