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The organometallic active site of [Fe]hydrogenase: Models and entatic states

2003; National Academy of Sciences; Volume: 100; Issue: 7 Linguagem: Inglês

10.1073/pnas.0536955100

1091-6490

Marcetta Y. Darensbourg, Erica J. Lyon, Xuan Zhao, Irene P. Georgakaki,

Catalysis for Biomass Conversion

The simple organometallic, (μ-S 2 )Fe 2 (CO) 6 , serves as a precursor to synthetic analogues of the chemically rudimentary iron-only hydrogenase enzyme active site. The fundamental properties of the (μ-SCH 2 CH 2 CH 2 S)[Fe(CO) 3 ] 2 compound, including structural mobility and regioselectivity in cyanide/carbon monoxide substitution reactions, relate to the enzyme active site in the form of transition-state structures along reaction paths rather than ground-state structures. Even in the absence of protein-based active-site organization, the ground-state structural model complexes are shown to serve as hydrogenase enzyme reaction models, H 2 uptake and H 2 production, with the input of photo- or electrochemical energy, respectively.