title: Artificial hydrogenases.
abstract: Decades of biophysical study on the hydrogenase (H(2)ase) enzymes have yielded sufficient information to guide the synthesis of analogs of their active sites. Three families of enzymes serve as inspiration for this work: the [FeFe]-H(2)ases, [NiFe]-H(2)ases, and [Fe]-H(2)ases, all of which feature iron centers bound to both CO and thiolate. Artificial H(2)ases affect the oxidation of H(2) and the reverse reaction, the reduction of protons. These reactions occur via the intermediacy of metal hydrides. The inclusion of amine bases within the catalysts is an important design feature that is emulated in related bioinspired catalysts. Continuing challenges are the low reactivity of H(2) toward biomimetic H(2)ases.
authors.affiliation: School of Chemical Sciences, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States.
authors.forename: Bryan E
authors.initials: BE
authors.lastname: Barton
authors.forename: Matthew T
authors.initials: MT
authors.lastname: Olsen
authors.forename: Thomas B
authors.initials: TB
authors.lastname: Rauchfuss
mesh_terms: D032701:Biomimetics; D006859:Hydrogen / Q000378:metabolism; D006864:Hydrogenase / Q000378:metabolism*; D007501:Iron / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000378:metabolism
chemical_list: D007506:Iron-Sulfur Proteins; D006859:Hydrogen; D007501:Iron; D006864:Hydrogenase