Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanism.
作者： Yuta Miki , Rebecca Pogni , Sandra Acebes , Fátima Lucas , Elena Fernández-Fueyo
DOI: 10.1042/BJ20130251
关键词:
摘要: LiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) instead of the tryptophan conserved in other lignin-degrading peroxidases. Pristine showed a lag period VA (veratryl alcohol) oxidation. However, VA-LiP (LiP after treatment with H2O2 and VA) lacked this lag, H2O2-LiP (H2O2-treated LiP) was inactive. MS analyses revealed that includes one molecule covalently bound to side chain Tyr181, whereas contains hydroxylated Tyr181. No adduct is formed Y171N variant. Molecular docking binding favoured by sandwich π stacking Tyr181 Phe89. EPR spectroscopy peroxide activation pre-treated LiPs protein radicals than radical found pristine LiP, which were assigned tyrosine-VA dihydroxyphenyalanine H2O2-LiP. Both are able oxidize large low-redox-potential substrates, but unable high-redox-potential substrates. Transient-state kinetics strongly promotes (>100-fold) substrate oxidation compound II, rate-limiting step catalysis. The novel mechanism involved ligninolysis, as demonstrated using lignin model present paper first report on autocatalytic modification, resulting functional alteration, among class II
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