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A new subfield of bioorganometallic chemistry is evolving, which derives from hydrogenase enzymes: metalloproteins containing low‐valent, first‐row transition metals within metal–metal binding distance and stabilized by the most classical of organometallic ligands, carbon monoxide. The review of the structures, mechanisms, and synthetic analogs of the active sites of [NiFe]‐, [FeFe]‐, and [Fe]‐hydrogenase...
Hydrogen is an energy vector with great potential, and the large‐scale development of hydrogen technologies currently relies on the catalytic properties of noble metals, making them both unsustainable and economically questionable. Alternative catalytic materials can be derived from hydrogenase enzymes or bio‐inspired molecular catalysts mimicking either the structure of their active site or their...
Enzymes are the catalysts of the living world. Nature has tailored proteins to catalyze an incredibly wide range of reactions with exquisite selectivity and efficiency under very mild conditions of temperature, pH, pressure, and so on. Protein engineering combined with molecular modeling techniques affords tailor‐made biocatalysts for the industrial production of chiral synthons. Nonetheless, endowing...
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