Related Experiment Video
Updated: Mar 25, 2026

Anaerobic Protein Purification and Kinetic Analysis via Oxygen Electrode for Studying DesB Dioxygenase Activity and Inhibition
Published on: October 3, 2018
Structure of Thermobifida fusca DyP-type peroxidase and activity towards Kraft lignin and lignin model compounds
Rahman Rahmanpour1, Dean Rea2, Shirin Jamshidi1
1Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry CV4 7AL, UK.
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.
Related Concept Videos
Oxidation of Phenols to Quinones
o-hydroxy phenols are oxidized to o-quinones and p-hydroxy phenols to p-quinones. Such redox reactions involve the transfer of two electrons and two protons. The reversible redox...
Oxidation of Alkenes: Syn Dihydroxylation with Potassium Permanganate
Reactions of Aldehydes and Ketones: Baeyer–Villiger Oxidation
The carbonyl center is activated by...
UV–Vis Spectroscopy: Woodward–Fieser Rules
Oxidation of Alkenes: Anti Dihydroxylation with Peroxy Acids

