5FW4

Structure of Thermobifida fusca DyP-type Peroxidase and Activity towards Kraft Lignin and Lignin Model Compounds

Summary for 5FW4

• Entry DOI: 10.2210/pdb5fw4/pdb
• Descriptor: DYE-DECOLORIZING PEROXIDASE TFU_3078, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total)
• Functional Keywords: oxidoreductase, decolorizing peroxidase, dyp, lignin oxidation
• Biological source: THERMOBIFIDA FUSCA
• Cellular location: Secreted : Q47KB1
• Total number of polymer chains: 2
• Total formula weight: 93261.85

Authors

Rahmanpour, R.,Rea, D.,Jamshidi, S.,Fulop, V.,Bugg, T.D.H. (deposition date: 2016-02-11, release date: 2016-04-06, Last modification date: 2024-01-10)

Primary citation

Rahmanpour, R.,Rea, D.,Jamshidi, S.,Fulop, V.,Bugg, T.D.H.
Structure of Thermobifida Fusca Dyp-Type Peroxidase and Activity Towards Kraft Lignin and Lignin Model Compounds.
Arch.Biochem.Biophys., 594:54-, 2016

PubMed 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.

PubMed: 26901432
DOI: 10.1016/J.ABB.2016.02.019

Experimental method

X-RAY DIFFRACTION (1.8 Å)