2 publications
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Generation of a Functional, Semisynthetic [FeFe]-Hydrogenase in a Photosynthetic Microorganism
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Energy Environ. Sci. 2018, 11, 3163-3167, 10.1039/C8EE01975D
[FeFe]-Hydrogenases are hydrogen producing metalloenzymes with excellent catalytic capacities, highly relevant in the context of a future hydrogen economy. Here we demonstrate the synthetic activation of a heterologously expressed [FeFe]-hydrogenase in living cells of Synechocystis PCC 6803, a photoautotrophic microbial chassis with high potential for biotechnological energy applications. H2-Evolution assays clearly show that the non-native, semi-synthetic enzyme links to the native metabolism in living cells.
Metal: FeHost protein: HydA1 ([FeFe]-hydrogenase) from C. reinhardtiiAnchoring strategy: ReconstitutionOptimization: Chemical & geneticNotes: ---
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Structure and Function in Organometallic Protein Complexes
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J. Organomet. Chem. 2014, 751, 90-110, 10.1016/j.jorganchem.2013.07.004
Bioorganometallic chemistry is a rapidly growing subfield of organometallic chemistry. One important facet is the study of organometallic•protein complexes that contain a covalent bond between the protein and an organometallic prosthetic group. Structural elucidation of these complexes is being used with increasing frequency to determine exactly where metal binding takes place and to obtain accurate structural information. This review summarizes the structures in this field, highlighting how this information has driven the frontier of this research.
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