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
Minimal and hybrid hydrogenases are active from archaea
Part of Cell, 2024
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
- Download full text (pdf) of Probing Substrate Transport Effects on Enzymatic Hydrogen Catalysis: An Alternative Proton Transfer Pathway in Putatively Sensory [FeFe] Hydrogenase
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
- Download full text (pdf) of Light-Driven [FeFe] Hydrogenase Based H-2 Production in E. coli: A Model Reaction for Exploring E. coli Based Semiartificial Photosynthetic Systems
Part of Advanced Synthesis and Catalysis, p. 2972-2981, 2022
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
Part of Cell Reports Physical Science, 2021
Part of ACS Catalysis, p. 9943-9952, 2020
Part of Advanced Synthesis and Catalysis, p. 812-821, 2020
Part of Chemical Science, p. 12789-12801, 2020
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
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
- Download full text (pdf) of B-factor Guided Proline Substitutions in Chromobacterium violaceum Amine Transaminase: Evaluation of the Proline Rule as a Method for Enzyme Stabilization
Discovery of novel [FeFe]-hydrogenases for biocatalytic H-2-production
Part of Chemical Science, p. 9941-9948, 2019