The organometallic active site of [Fe]hydrogenase: models and entatic states.
The simple organometallic, (mu-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 (mu-SCH(2)CH(2)CH(2)S)[Fe(CO)(3)](2) compound, including structural mobility and regioselectivity in cyanidecarbon 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.
Darensbourg
Marcetta Y
MY
Texas A&M University, Department of Chemistry, College Station, TX 77843, USA. marcetta@mail.chem.tamu.edu
Lyon
Erica J
EJ
Zhao
Xuan
X
Georgakaki
Irene P
IP
D001665:Binding Sites; D006859:Hydrogen / Q000378:metabolism; D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism*; D007506:Iron-Sulfur Proteins / Q000737:chemistry* / Q000378:metabolism*; D007700:Kinetics; D008958:Models, Molecular; D009942:Organometallic Compounds / Q000737:chemistry*; D017433:Protein Structure, Secondary
D007506:Iron-Sulfur Proteins; D009942:Organometallic Compounds; D006859:Hydrogen; C118830:iron hydrogenase; D006864:Hydrogenase