projects
Snapshot of what we are building, from metalloenzymes to spectroscopy platforms.
Research overview
We operate at the interface of biology and physics to understand how metalloenzymes control redox chemistry. Our strategy mixes molecular biology, structural biology, spectroscopy, and computation so we can connect macromolecular structure to electronic structure.
Current focus areas
COOFIX · FRIPRO (Research Council of Norway, 2020–2026)
Designing and evolving copper enzymes that reduce CO2. We combine directed evolution, structural biology, and electronic-structure calculations to map new catalytic pathways.
CUBE – ERC Synergy Grant (2020–2026)
Joint effort on Cu-based catalysts for C–H activation and selective oxidation. We co-lead spectroscopy, mechanistic modelling, and data pipelines that explain how catalyst microenvironments govern reactivity.
Lytic polysaccharide monooxygenases
Mechanistic studies of AA9/AA14 LPMOs and related type-3 copper proteins. We resolve hole hopping, substrate binding, and reductant control using spectroscopy, QM/MM, and MD simulations.
Flavoenzymes
Flavodoxins and flavin reductases that shuttle electrons to LPMOs. We probe their fast redox cycles and compatibility with biorefinery process streams.
Structural biology & computational chemistry
Protein crystallography, multi-scale simulations, and in-house workflows that couple QM, MM, and machine-learned potentials to experimental observables.
Finalized collaborative projects
- OXYMOD – Digital Life Norway (2017–2022): Partnered on oxidative enzyme cascades for lignocellulose conversion.
- FRIPRO 240967 (2015–2019): Led the combined computational/experimental campaign that still underpins our LPMO toolset.
Methods toolbox
- Spectroscopy: EPR, Raman, UV-Vis, fluorescence, stopped-flow kinetics.
- Robotics & automation: Custom liquid-handling for crystallization and enzyme evolution.
- Computation: High-performance QM/MM, MD, and bespoke analysis pipelines on Sigma2 and local GPU clusters.