Recombinant and in vitro expression systems for hydrogenases: new frontiers in basic and applied studies for biological and synthetic H2 production
- 27 October 2009
- journal article
- review article
- Published by Royal Society of Chemistry (RSC) in Dalton Transactions
- No. 45,p. 9970-9978
- https://doi.org/10.1039/b913426n
Abstract
This review focuses on recent progress in developing heterologous and recombinant expression as well as in vitro maturation systems for the biosynthesis of active [FeFe] and [NiFe]-hydrogenases, which catalyze the reversible reaction, H2↔ 2e− + 2H+ . Activities of [FeFe] and [NiFe]-hydrogenases produced from different recombinant and in vitro maturation approaches are compared. Examples of how hydrogenase expression supports basic and applied studies of these enzymes are presented, and barriers to achieving more viable biological and synthetic H2-production systems and catalysts are addressed.Keywords
This publication has 128 references indexed in Scilit:
- Visible light driven H2 production in molecular systems employing colloidal MoS2 nanoparticles as catalystChemical Communications, 2009
- Hydrogen Production by a Hyperthermophilic Membrane-Bound Hydrogenase in Water-Soluble Nanolipoprotein ParticlesJournal of the American Chemical Society, 2009
- Experimental approaches to kinetics of gas diffusion in hydrogenaseProceedings of the National Academy of Sciences, 2008
- Potential for hydrogen production with inducible chloroplast gene expression in ChlamydomonasProceedings of the National Academy of Sciences, 2007
- Occurrence, Classification, and Biological Function of Hydrogenases: An OverviewChemical Reviews, 2007
- Maturation of [NiFe]-hydrogenases in Escherichia coliBioMetals, 2007
- Photoinduced Hydrogen Production by Direct Electron Transfer from Photosystem I Cross-Linked with Cytochrome c3to [NiFe]-HydrogenasePhotochemistry and Photobiology, 2006
- Sequential and structural analysis of [NiFe]-hydrogenase-maturation proteins from Desulfovibrio vulgaris Miyazaki FAntonie van Leeuwenhoek, 2006
- The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygenJBIC Journal of Biological Inorganic Chemistry, 2004
- Characterization of the periplasmic hydrogenase from Desulfovibrio gigasBiochemical and Biophysical Research Communications, 1978