title: Bioelectrocatalytic properties of lignin peroxidase from Phanerochaete chrysosporium in reactions with phenols, catechols and lignin-model compounds.
abstract: Bioelectrocatalytic reduction of H(2)O(2) catalysed by lignin peroxidase from Phanerochaete chrysosporium (LiP) was studied with LiP-modified graphite electrodes to elucidate the ability of LiP to electro-enzymatically oxidise phenols, catechols, as well as veratryl alcohol (VA) and some other high-redox-potential lignin model compounds (LMC). Flow-through amperometric experiments performed at +0.1 V vs. Ag|AgCl demonstrated that LiP displayed significant bioelectrocatalytic activity for the reduction of H(2)O(2) both directly (i.e., in direct electron transfer (ET) reaction between LiP and the electrode) and using most of studied compounds acting as redox mediators in the LiP bioelectrocatalytic cycle, with a pH optimum of 3.0. The bioelectrocatalytic reduction of H(2)O(2) mediated by VA and effects of VA on the efficiency of bioelectrocatalytic oxidation of other co-substrates acting as mediators were investigated. The bioelectrocatalytic oxidation of phenol- and catechol derivatives and 2,2'-azino-bis(3-ethyl-benzothiazoline-6-sulphonate) by LiP was independent of the presence of VA, whereas the efficiency of the LiP bioelectrocatalysis with the majority of other LMC acting as mediators increased upon addition of VA. Special cases were phenol and 4-methoxymandelic acid (4-MMA). Both phenol and 4-MMA suppressed the bioelectrocatalytic activity of LiP below the direct ET level, which was, however, restored and increased in the presence of VA mediating the ET between LiP and these two compounds. The obtained results suggest different mechanisms for the bioelectrocatalysis of LiP depending on the chemical nature of the mediators and are of a special interest both for fundamental science and for application of LiP in biotechnological processes as solid-phase bio(electro)catalyst for decomposition/detection of recalcitrant aromatic compounds.
authors.affiliation: School of Chemistry, College of Science and Engineering, the University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, UK. elena.ferapontova@ed.ac.uk
authors.forename: Elena E
authors.initials: EE
authors.lastname: Ferapontova
authors.forename: John
authors.initials: J
authors.lastname: Castillo
authors.forename: Lo
authors.initials: L
authors.lastname: Gorton
mesh_terms: D002384:Catalysis; D002396:Catechols / Q000737:chemistry / Q000378:metabolism*; D004566:Electrodes; D004583:Electrons; D004800:Enzymes, Immobilized / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000737:chemistry / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008031:Lignin / Q000737:chemistry* / Q000378:metabolism*; D008954:Models, Biological; D015394:Molecular Structure; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000378:metabolism*; D020075:Phanerochaete / Q000201:enzymology*; D010636:Phenols / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity
chemical_list: D002396:Catechols; D004800:Enzymes, Immobilized; D010636:Phenols; D008031:Lignin; D006861:Hydrogen Peroxide; D010544:Peroxidases; C042858:lignin peroxidase; C034221:catechol