Kjendseth Lab
Norwegian University of Life Sciences (NMBU) · Faculty of Chemistry, Biotechnology and Food Science (KBM)
Åsmund Røhr Kjendseth leads the Kjendseth Lab at NMBU’s Faculty of Chemistry, Biotechnology and Food Science, where he also serves as Head of Education and Leader for the Chemistry research group (about 20 members). We mix robotics, spectroscopy, and computation to explain how redox enzymes remodel biomass and point the way to resilient biocatalysts.
Research focus
- Redox chemistry and reaction pathways of copper enzymes
- Spectroscopic probes for enzyme intermediates and oxygen activation
- Computational workflows that integrate quantum chemical and molecular simulations with experiment
- Enzyme engineering strategies employing state-of-the-art AI tools and HPC
Highlights
- Leads projects with NMBU and US partners on carbon-negative catalysis and enzymatic biomass conversion.
- Principal Investigator on the FRIPRO-funded COOFIX programme and co-PI on the ERC Synergy grant CUBE.
- Builds multidisciplinary team that span automatization, spectroscopy, structural biology, and computational chemistry.
news
| Aug 05, 2025 | New publication out in Biochemistry detailing the activity of a cryptic Pseudomonas aeruginosa prophage endolysin (doi:10.1021/acs.biochem.5c00142). Great work by Per Kristian Thorén Edvardsen, Andrea Nikoline Englund, and collaborators across KBM and beyond. |
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| Feb 07, 2025 | Åsmund shared recent spectroscopy results and computational insights during the Hylleraas Centre seminar in Oslo, highlighting how experiments guide our understanding of LPMO redox chemistry. (Source: Hylleraas Centre event listing.) |
| May 10, 2024 | Nature Communications paper on hole hopping in LPMOs |
selected publications
- Biophys. J.The rotamer of the second-sphere histidine in AA9 lytic polysaccharide monooxygenase is pH dependentBiophysical Journal, 2024
- ACS Catal.Structure-Function Analysis of an Understudied Type of LPMO with Unique Redox Properties and Substrate SpecificityACS Catalysis, 2025
- Nat. Commun.Mutational dissection of a hole hopping route in a lytic polysaccharide monooxygenase (LPMO)Nature Communications, 2024