title: Bio-inspired mechanistic insights into CO₂ reduction.
abstract: The global energy and environmental concerns related to the excess CO2 concentration in the atmosphere have intensified the research and development regarding CO2 utilization. Due to the high stability and inertness of CO2, CO2 functionalization under mild conditions has been proven to be extremely challenging. Nature has, however, evolved efficient pathways to achieve this difficult transformation. Herein, we compare the mechanisms of CO2 two-electron reduction followed by synthetic catalysts and those by carbon monoxide dehydrogenase and formate dehydrogenase in order to provide more mechanistic insights into future catalyst design.
authors.affiliation: Max-Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
authors.forename: Bhaskar
authors.initials: B
authors.lastname: Mondal
authors.affiliation: Max-Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
authors.forename: Jinshuai
authors.initials: J
authors.lastname: Song
authors.affiliation: Max-Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany.
authors.forename: Frank
authors.initials: F
authors.lastname: Neese
authors.affiliation: Max-Planck Institute for Chemical Energy Conversion, Stiftstrasse 34-36, D-45470 Mülheim an der Ruhr, Germany. Electronic address: shengfa.ye@cec.mpg.de.
authors.forename: Shengfa
authors.initials: S
authors.lastname: Ye
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000378:metabolism; D032701:Biomimetics / Q000379:methods*; D002245:Carbon Dioxide / Q000737:chemistry* / Q000378:metabolism; D002384:Catalysis; D004579:Electron Transport; D005560:Formate Dehydrogenases / Q000378:metabolism; D009097:Multienzyme Complexes / Q000378:metabolism
chemical_list: D009097:Multienzyme Complexes; D002245:Carbon Dioxide; D005560:Formate Dehydrogenases; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase