ReviewJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2021
Aspartate or arginine? Validated redox state X-ray structures elucidate mechanistic subtleties of Fe
Review in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 27 citations in OpenAlex.
- Can ferric-oxyl excited states explain elongated iron-oxygen bonds in heme peroxidase catalytic intermediates?Nature communications · 2026Article
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- Damage before destruction? X-ray-induced changes in single-pulse serial femtosecond crystallography.IUCrJ · 2025Article
- The oligomeric states of dye-decolorizing peroxidases from Streptomyces lividans and their implications for mechanism of substrate oxidation.Protein science : a publication of the Protein Society · 2024Article
- Dye-Decolorizing Peroxidase ofACS omega · 2024Article
- Biochemical, Biophysical, and Structural Analysis of an Unusual DyP from the ExtremophileMolecules (Basel, Switzerland) · 2024Article
- Spectroelectrochemistry for determination of the redox potential in heme enzymes: Dye-decolorizing peroxidases.BBA advances · 2024Article
- New insights into controlling radical migration pathways in heme enzymes gained from the study of a dye-decolorising peroxidase.Chemical science · 2023Article
- Comprehensive structural, infrared spectroscopic and kinetic investigations of the roles of the active-site arginine in bidirectional hydrogen activation by the [NiFe]-hydrogenase 'Hyd-2' fromChemical science · 2023Article
- A bacterial cold-active dye-decolorizing peroxidase from an Antarctic Pseudomonas strain.Applied microbiology and biotechnology · 2023Article
- Perspective: Structure determination of protein-ligand complexes at room temperature using X-ray diffraction approaches.Frontiers in molecular biosciences · 2023Article
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- Article
- Unveiling molecular details behind improved activity at neutral to alkaline pH of an engineered DyP-type peroxidase.Computational and structural biotechnology journal · 2022Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Structure determination of proteins and enzymes by X-ray crystallography remains the most widely used approach to complement functional and mechanistic studies. Capturing the structures of intact redox states in metalloenzymes is critical for assigning the chemistry carried out by the metal in the catalytic cycle. Unfortunately, X-rays interact with protein crystals to generate solvated photoelectrons that can reduce redox active metals and hence change the coordination geometry and the coupled protein structure. Approaches to mitigate such site-specific radiation damage continue to be developed, but nevertheless application of such approaches to metalloenzymes in combination with mechanistic studies are often overlooked. In this review, we summarize our recent structural and kinetic studies on a set of three heme peroxidases found in the bacterium Streptomyces lividans that each belong to the dye decolourizing peroxidase (DyP) superfamily. Kinetically, each of these DyPs has a distinct reactivity with hydrogen peroxide. Through a combination of low dose synchrotron X-ray crystallography and zero dose serial femtosecond X-ray crystallography using an X-ray free electron laser (XFEL), high-resolution structures with unambiguous redox state assignment of the ferric and ferryl (Fe
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