Skip to Main Content
Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanismAuthor(s): Yuta Miki; Rebecca Pogni; Sandra Acebes; Fatima Lucas; Elena Fernandez-Fueyo; Maria Camilla Baratto; Maria I. Fernandez; Vivian De Los Rios; Francisco J. Ruiz-duenas; Adalgisa Sinicropi; Riccardo Basosi; Kenneth E. Hammel; Victor Guallar; Angel T. Martinez
Source: Biochem. J. Volume, 452, 2013; pp. 575-584.
Publication Series: Scientific Journal (JRNL)
Station: Forest Products Laboratory
Download Publication (1.52 MB)
DescriptionLiP (lignin peroxidase) from Trametopsis cervina has an exposed catalytic tyrosine residue (Tyr181) instead of the tryptophan conserved in other lignin-degrading peroxidases. Pristine LiP showed a lag period in VA (veratryl alcohol) oxidation. However, VA-LiP (LiP after treatment with H2O2 and VA) lacked this lag, and H2O2-LiP (H2O2-treated LiP) was inactive. MS analyses revealed that VA-LiP includes one VA molecule covalently bound to the side chain of Tyr181, whereas H2O2-LiP contains a hydroxylated Tyr181. No adduct is formed in the Y171N variant. Molecular docking showed that VA binding is favoured by sandwich π stacking with Tyr181 and Phe89. EPR spectroscopy after peroxide activation of the pre-treated LiPs showed protein radicals other than the tyrosine radical found in pristine LiP,which were assigned to a tyrosine–VA adduct radical in VA-LiP and a dihydroxyphenyalanine radical in H2O2-LiP. Both radicals are able to oxidize large low-redox-potential substrates, but H2O2-LiP is unable to oxidize high-redox-potential substrates. Transientstate kinetics showed that the tyrosine–VA adduct strongly promotes (>100-fold) substrate oxidation by compound II, the rate-limiting step in catalysis. The novel activation mechanism is involved in ligninolysis, as demonstrated using lignin model substrates. The present paper is the first report on autocatalytic modification, resulting in functional alteration, among class II peroxidases.
- We recommend that you also print this page and attach it to the printout of the article, to retain the full citation information.
- This article was written and prepared by U.S. Government employees on official time, and is therefore in the public domain.
CitationMiki, Yuta; Pogni, Rebecca; Acebes, Sandra; Lucas, Fatima; Fernandez-Fueyo, Elena; Baratto, Maria Camilla; Fernandez, Maria I.; Rios, Vivian De Los; Ruiz-duenas, Francisco J.; Sinicropi, Adalgisa; Basosi, Riccardo; Hammel, Kenneth E.; Guallar, Victor; Martinez, Angel T. 2013. Formation of a tyrosine adduct involved in lignin degradation by Trametopsis cervina lignin peroxidase: a novel peroxidase activation mechanism. Biochemical Journal. 452: 575-584.
KeywordsEPR, lignin model compound, lignin peroxidase (LiP), molecular docking, MS, quantum mechanics/molecular mechanics (QM/MM), tyrosine adduct
- Fungal lignin peroxidase does not produce the veratryl alcohol cation radical as a diffusible ligninolytic oxidant
- Peroxyl radicals are potential agents of lignin biodegradation
- Oxidizability of unsaturated fatty acids and of a non-phenolic lignin structure in the manganese peroxidase-dependent lipid peroxidation system
XML: View XML