A new versatile peroxidase from Pleurotus. (May 2001)

• Record Type: Journal Article
• Authors: Ruiz-Dueñas, F. J.; Camarero, S.; Pérez-Boada, M.; Martínez, M. J.; Martínez, A. T.
• Is Part Of: Biochemical Society transactions. Volume 29:Number 2(2001)
• Page Start: 116
• Page End: 122
• Publication Date: 2001-05
• Subjects: aromatic substrates -- ligninolytic peroxidases -- long-range electron transfer -- substrate-interaction sites -- white-rot fungi; ABTS, 2, 2′-azinobis-(3-ethylbenzothiazoline-6-sulphonate) -- CIP, Coprinus cinereus peroxidase -- LiP, lignin peroxidase -- MnP, manganese peroxidase -- MRP, Mn-repressed peroxidase -- RB5, Reactive Black 5 -- SDM, site-directed mutagenesis -- VA, veratryl alcohol -- VP, versatile peroxidase -- LRET, long-range electron transfer; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0290116
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been investigated in Phanero-chaete chrysosporium. A third ligninolytic peroxidase has been described in Pleurotus and Bjerkandera. Two of these versatile peroxidases (VPs) have been cloned, sequenced and characterized. They have high affinity for Mn 2+, hydro-quinones and dyes, and also oxidize veratryl alcohol, dimethoxybenzene and lignin dimers. The deduced sequences show higher identity with Ph. chrysosporium LiP than MnP, but the molecular models obtained include a Mn 2+ -binding site. Concerning aromatic substrate oxidation, Pl. eryngii VP shows a putative long-range electron transfer pathway from an exposed trytophan to haem. Mutagenesis and chemical modification of this tryptophan and the acidic residues forming the Mn 2+ -binding site confirmed their role in catalysis. The existence of several substrate oxidation sites is supported further by biochemical evidence. Residue conservation in other fungal peroxidases is discussed.