| Literature DB >> 26901432 |
Rahman Rahmanpour1, Dean Rea2, Shirin Jamshidi1, Vilmos Fülöp2, Timothy D H Bugg3.
Abstract
A Dyp-type peroxidase enzyme from thermophilic cellulose degrader Thermobifida fusca (TfuDyP) was investigated for catalytic ability towards lignin oxidation. TfuDyP was characterised kinetically against a range of phenolic substrates, and a compound I reaction intermediate was observed via pre-steady state kinetic analysis at λmax 404 nm. TfuDyP showed reactivity towards Kraft lignin, and was found to oxidise a β-aryl ether lignin model compound, forming an oxidised dimer. A crystal structure of TfuDyP was determined, to 1.8 Å resolution, which was found to contain a diatomic oxygen ligand bound to the heme centre, positioned close to active site residues Asp-203 and Arg-315. The structure contains two channels providing access to the heme cofactor for organic substrates and hydrogen peroxide. Site-directed mutant D203A showed no activity towards phenolic substrates, but reduced activity towards ABTS, while mutant R315Q showed no activity towards phenolic substrates, nor ABTS.Entities:
Keywords: Dye decolorizing peroxidase; Dyp; Lignin oxidation; Protein crystallography
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Year: 2016 PMID： 26901432 DOI： 10.1016/j.abb.2016.02.019
Source DB: PubMed Journal: Arch Biochem Biophys ISSN： 0003-9861 Impact factor: 4.013