Henrik Land
Associate senior lecturer/Assistant Professor at Department of Chemistry - Ångström Laboratory; Molecular Biomimetics; Biophysical and Bioinorganic Chemistry
- E-mail:
- henrik.land@kemi.uu.se
- Visiting address:
- Ångströmlaboratoriet, Lägerhyddsvägen 1
75120 Uppsala - Postal address:
- Box 523
75120 Uppsala

Publications
Recent publications
Part of eLIFE, 2026
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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A widespread hydrogenase supports fermentative growth of gut bacteria in healthy people
Part of Nature Microbiology, p. 2686-2701, 2025
- DOI for A widespread hydrogenase supports fermentative growth of gut bacteria in healthy people
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Part of Microbial Cell Factories, 2025
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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All publications
Articles in journal
Part of eLIFE, 2026
Part of Microbial Cell Factories, 2025
- DOI for Structure-guided engineering of α-ketoisocaproate dioxygenase increases isobutene production in Synechocystis sp. PCC 6803
- Download full text (pdf) of Structure-guided engineering of α-ketoisocaproate dioxygenase increases isobutene production in Synechocystis sp. PCC 6803
A widespread hydrogenase supports fermentative growth of gut bacteria in healthy people
Part of Nature Microbiology, p. 2686-2701, 2025
- DOI for A widespread hydrogenase supports fermentative growth of gut bacteria in healthy people
- Download full text (pdf) of A widespread hydrogenase supports fermentative growth of gut bacteria in healthy people
Part of Microbial Cell Factories, 2025
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
- Download full text (pdf) of Indications for a universal hydrogen catalysis mechanism in [FeFe]-hydrogenases of different phylogenetic groups
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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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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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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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 Advanced Synthesis and Catalysis, p. 2972-2981, 2022
- DOI for Enantioselective Synthesis of Pharmaceutically Relevant Bulky Arylbutylamines Using Engineered Transaminases
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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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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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Reversible or Irreversible Catalysis of H+/H2 Conversion by FeFe Hydrogenases
Part of Journal of the American Chemical Society, p. 20320-20325, 2021
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 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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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 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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Current State of [FeFe]-Hydrogenase Research: Biodiversity and Spectroscopic Investigations
Part of ACS Catalysis, p. 7069-7086, 2020
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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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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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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