ArticleScientific reports2019
Trp-His covalent adduct in bilirubin oxidase is crucial for effective bilirubin binding but has a minor role in electron transfer.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- A la carte bioprospecting of substrate-selective laccases via high-throughput computational enzyme-substrate interaction profiling.Protein science : a publication of the Protein Society · 2026Article
- Electrochemical Small-Angle X-ray Scattering for Potential-Dependent Structural Analysis of Redox Enzymes.Langmuir : the ACS journal of surfaces and colloids · 2025Article
- Improving macromolecular structure refinement with metal-coordination restraints.Acta crystallographica. Section D, Structural biology · 2024Article
- Biochemical and Structural Characterization of a Novel Psychrophilic Laccase (Multicopper Oxidase) Discovered fromInternational journal of molecular sciences · 2024Article
- The Structure of Bilirubin Oxidase fromBiosensors · 2022Article
- Modelling covalent linkages in CCP4.Acta crystallographica. Section D, Structural biology · 2021Article
- Paired refinement under the control ofIUCrJ · 2020Article
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11 authors at 2 institutions in 2 countries.
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Abstract
Unlike any protein studied so far, the active site of bilirubin oxidase from Myrothecium verrucaria contains a unique type of covalent link between tryptophan and histidine side chains. The role of this post-translational modification in substrate binding and oxidation is not sufficiently understood. Our structural and mutational studies provide evidence that this Trp396-His398 adduct modifies T1 copper coordination and is an important part of the substrate binding and oxidation site. The presence of the adduct is crucial for oxidation of substituted phenols and it substantially influences the rate of oxidation of bilirubin. Additionally, we bring the first structure of bilirubin oxidase in complex with one of its products, ferricyanide ion, interacting with the modified tryptophan side chain, Arg356 and the active site-forming loop 393-398. The results imply that structurally and chemically distinct types of substrates, including bilirubin, utilize the Trp-His adduct mainly for binding and to a smaller extent for electron transfer.
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