Senger Group

A collage of crystal structures, reaction formulas and data reminiscent of enzymatic catalysis.

Molecular mechanisms of enzymatic catalysis for sustainable development

In our group we try to make a positive difference in society through beyond state-of-the-art research on enzymatic catalysis mechanisms to replace fossil resources with sustainable alternatives. Inspired by Nature we target production of hydrogen as a green fuel, carbon dioxide fixation to higher products and nitrogen conversion into ammonia as a fertiliser.

We focus on the structure function relationship in proteins and our work spans from expression, purification and crystallisation of proteins over their biochemical and extended biophysical characterisation to photochemical activation and advanced structure determination using synchrotron and Free Electron Laser X-ray sources.

Read more about our research

Group members

Research leader: Moritz Senger

Group members: Laura Kiesewetter, Robin Stipp, Ivan Voloshyn

Publications

Beyond Canonical CO Oxidation: First Characterisation of a Clade B CODH using a New Anaerobic Cryo-EM Workflow

Böhm, Maximilian; Srinivas, Vivek; Wiseman, Benjamin; Huang, Ping et al.

2026
- Download full text (pdf) of Beyond Canonical CO Oxidation: First Characterisation of a Clade B CODH using a New Anaerobic Cryo-EM Workflow
Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved H₂ Evolution and O₂ Tolerance through Rational Design of [FeFe] Hydrogenase

Cabotaje, Princess R.; Sekretareva, Alina; Senger, Moritz; Huang, Ping et al.

Part of Journal of the American Chemical Society, p. 4654-4666, 2025
- DOI for Probing the Influence of the Protein Scaffold on H-Cluster Reactivity via Gain-of-Function Studies─Improved H₂ Evolution and O₂ Tolerance through Rational Design of [FeFe] Hydrogenase
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Indications for a universal hydrogen catalysis mechanism in [FeFe]-hydrogenases of different phylogenetic groups

Senger, Moritz; Schumann, Conrad; Cabotaje, Princess R.; Zamader, Afridi et al.

Part of Physical Chemistry, Chemical Physics - PCCP, p. 9864-9875, 2025
- DOI for Indications for a universal hydrogen catalysis mechanism in [FeFe]-hydrogenases of different phylogenetic groups
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Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays

Sönmez, Eda; Kostopoulos, Nikolaos; Gamache, Mira; Cheah, Mun Hon et al.

Part of Analytical Chemistry, p. 26393-26403, 2025
- DOI for Reconsidering the Enzyme Kinetics of [FeFe]-Hydrogenases: Improved Turnover Rates and New Insights into pH and Potential Dependence with Eu(II)-Based Solution Assays
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Secondary structure changes as the potential H₂ sensing mechanism of group D [FeFe]-hydrogenases

Voloshyn, Ivan; Schumann, Conrad; Cabotaje, Princess R.; Zamader, Afridi et al.

Part of Chemical Communications, p. 10914-10917, 2024
- DOI for Secondary structure changes as the potential H₂ sensing mechanism of group D [FeFe]-hydrogenases
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Minimal and hybrid hydrogenases are active from archaea

Greening, Chris; Cabotaje, Princess R.; Valentin Alvarado, Luis E.; Leung, Pok Man et al.

Part of Cell, 2024
- DOI for Minimal and hybrid hydrogenases are active from archaea
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Structural basis for bacterial energy extraction from atmospheric hydrogen

Grinter, Rhys; Kropp, Ashleigh; Venugopal, Hari; Senger, Moritz et al.

Part of Nature, p. 541-547, 2023
- DOI for Structural basis for bacterial energy extraction from atmospheric hydrogen
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Elucidating Electron Transfer Kinetics and Optimizing System Performance for Escherichia coli-Based Semi-Artificial H-2 Production

Gamache, Mira T.; Charaf, Rima; Kurth, Larissa; Filmon, Dawit T. et al.

Part of ACS Catalysis, p. 9476-9486, 2023
- DOI for Elucidating Electron Transfer Kinetics and Optimizing System Performance for Escherichia coli-Based Semi-Artificial H-2 Production
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Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase

Cabotaje, Princess R.; Walter, Kaija; Zamader, Afridi; Huang, Ping et al.

Part of ACS Catalysis, p. 10435-10446, 2023
- DOI for Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase
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Polymer Dots as Photoactive Membrane Vesicles for [FeFe]-Hydrogenase Self-Assembly and Solar-Driven Hydrogen Evolution

Pavliuk, Mariia V.; Lorenzi, Marco; Morado, Dustin R.; Gedda, Lars et al.

Part of Journal of the American Chemical Society, p. 13600-13611, 2022
- DOI for Polymer Dots as Photoactive Membrane Vesicles for [FeFe]-Hydrogenase Self-Assembly and Solar-Driven Hydrogen Evolution
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Trapping an Oxidized and Protonated Intermediate of the [FeFe]-Hydrogenase Cofactor under Mildly Reducing Conditions

Senger, Moritz; Duan, Jifu; Pavliuk, Mariia V.; Apfel, Ulf-Peter et al.

Part of Inorganic Chemistry, p. 10036-10042, 2022
- DOI for Trapping an Oxidized and Protonated Intermediate of the [FeFe]-Hydrogenase Cofactor under Mildly Reducing Conditions
Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H-2 supports its catalytic relevance

Senger, Moritz; Kernmayr, Tobias; Lorenzi, Marco; Redman, Holly J. et al.

Part of Chemical Communications, p. 7184-7187, 2022
- DOI for Hydride state accumulation in native [FeFe]-hydrogenase with the physiological reductant H-2 supports its catalytic relevance
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Light-Driven [FeFe] Hydrogenase Based H-2 Production in E. coli: A Model Reaction for Exploring E. coli Based Semiartificial Photosynthetic Systems

Lorenzi, Marco; Gamache, Mira T.; Redman, Holly J.; Land, Henrik et al.

Part of ACS Sustainable Chemistry and Engineering, p. 10760-10767, 2022
- DOI for Light-Driven [FeFe] Hydrogenase Based H-2 Production in E. coli: A Model Reaction for Exploring E. coli Based Semiartificial Photosynthetic Systems
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Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site

Lorenzi, Marco; Gellett, Joe; Zamader, Afridi; Senger, Moritz et al.

Part of Chemical Science, p. 11058-11064, 2022
- DOI for Investigating the role of the strong field ligands in [FeFe] hydrogenase: spectroscopic and functional characterization of a semi-synthetic mono-cyanide active site
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Photosynthetic hydrogen production: Novel protocols, promising engineering approaches and application of semi‐synthetic hydrogenases

Kosourov, Sergey; Böhm, Maximilian; Senger, Moritz; Berggren, Gustav et al.

Part of Physiologia Plantarum, p. 555-567, 2021
- DOI for Photosynthetic hydrogen production: Novel protocols, promising engineering approaches and application of semi‐synthetic hydrogenases
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Site-selective protonation of the one-electron reduced cofactor in [FeFe]-hydrogenase

Laun, Konstantin; Baranova, Iuliia; Duan, Jifu; Kertess, Leonie et al.

Part of Dalton Transactions, p. 3641-3650, 2021
- DOI for Site-selective protonation of the one-electron reduced cofactor in [FeFe]-hydrogenase
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Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations

Land, Henrik; Senger, Moritz; Berggren, Gustav; Stripp, Sven T.

Part of ACS Catalysis, p. 7069-7086, 2020
- DOI for Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations
Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture

Land, Henrik; Sekretaryova, Alina N.; Huang, Ping; Redman, Holly J. et al.

Part of Chemical Science, p. 12789-12801, 2020
- DOI for Characterization of a putative sensory [FeFe]-hydrogenase provides new insight into the role of the active site architecture
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[FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy

Németh, Brigitta; Senger, Moritz; Redman, Holly J.; Ceccaldi, Pierre et al.

Part of Journal of Biological Inorganic Chemistry, p. 777-788, 2020
- DOI for [FeFe]-hydrogenase maturation: H-cluster assembly intermediates tracked by electron paramagnetic resonance, infrared, and X-ray absorption spectroscopy
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