Land group

Discovery and protein engineering of redox active metalloenzymes.
Our research
The Land group focuses on discovery and protein engineering of redox active metalloenzymes. Our research is interdisciplinary and combines protein engineering, bioinorganic chemistry and biophysics on enzymes that catalyze environmentally relevant reactions.
Our lab houses an uninterrupted anaerobic platform for screening of enzyme libraries that enables directed evolution of oxygen sensitive enzymes. This includes the ability to perform anaerobic protein expression, cell harvest and spectrophotometric analysis.
Group members
Publications
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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Part of Microbial Cell Factories, 2025
- DOI for Structure-guided engineering of α-ketoisocaproate dioxygenase increases isobutene production in Synechocystis sp. PCC 6803
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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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Minimal and hybrid hydrogenases are active from archaea
Part of Cell, 2024
- DOI for Minimal and hybrid hydrogenases are active from archaea
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Part of Chemical Science, p. 16789-16795, 2024
- DOI for Photobiocatalytic CO2 reduction into CO by organic nanorod-carbon monoxide dehydrogenase assemblies: surfactant matters
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Secondary structure changes as the potential H2 sensing mechanism of group D [FeFe]-hydrogenases
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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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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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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Part of Advanced Synthesis and Catalysis, p. 2972-2981, 2022
- DOI for Enantioselective Synthesis of Pharmaceutically Relevant Bulky Arylbutylamines Using Engineered Transaminases
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Reversible or Irreversible Catalysis of H+/H2 Conversion by FeFe Hydrogenases
Part of Journal of the American Chemical Society, p. 20320-20325, 2021
Semi-synthetic hydrogenases—in vitro and in vivo applications
Part of Current Opinion in Green and Sustainable Chemistry, 2021
- DOI for Semi-synthetic hydrogenases—in vitro and in vivo applications
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Part of Cell Reports Physical Science, 2021
- DOI for Semisynthetic [FeFe]-hydrogenase with stable expression and H2 production capacity in a photosynthetic microbe
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Part of ACS Catalysis, p. 9943-9952, 2020
- DOI for Carbon Dots and [FeFe] Hydrogenase Biohybrid Assemblies for Efficient Light-Driven Hydrogen Evolution
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Part of Advanced Synthesis and Catalysis, p. 812-821, 2020
- DOI for Engineering the Active Site of an (S)-Selective Amine Transaminase for Acceptance of Doubly Bulky Primary Amines
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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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Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations
Part of ACS Catalysis, p. 7069-7086, 2020
The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
Part of Journal of Biological Chemistry, p. 11891-11901, 2020
- DOI for The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
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Part of ChemBioChem, p. 1297-1304, 2019
- DOI for B-factor Guided Proline Substitutions in Chromobacterium violaceum Amine Transaminase: Evaluation of the Proline Rule as a Method for Enzyme Stabilization
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Discovery of novel [FeFe]-hydrogenases for biocatalytic H-2-production
Part of Chemical Science, p. 9941-9948, 2019
- DOI for Discovery of novel [FeFe]-hydrogenases for biocatalytic H-2-production
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