Resin-bound models of the [FeFe]-hydrogenase enzyme active site and studies of their reactivity.
The immobilization of synthetic analogues of the [FeFe]-hydrogenase, [FeFe]H(2)ase, enzyme active site on polyethyleneglycol-rich polystyrene beads is described. Using the reactivity of the amine termini of the PEG chains with carboxylates incorporated into (mu-SRS)[Fe(CO)(3)](2) or (mu-SR)(2)[Fe(CO)(3)](2) derivative, nu(CO)IR signatures can be used to interrogate the structure and properties of the diiron carbonyl complexes once incorporated into the PEG environment of the polymer beads. Alternatively, the SRS dithiolate was first attached to the resin and the diiron unit assembled via an in situ process on the bead.
Green
Kayla N
KN
Texas A & M University, Department of Chemistry, College Station, Texas 77843, USA.
Hess
Jennifer L
JL
Thomas
Christine M
CM
Darensbourg
Marcetta Y
MY
D032701:Biomimetics; D020134:Catalytic Domain; D003486:Cyanides / Q000737:chemistry; D006864:Hydrogenase / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D015394:Molecular Structure; D009942:Organometallic Compounds / Q000138:chemical synthesis / Q000737:chemistry*; D011092:Polyethylene Glycols / Q000737:chemistry; D012117:Resins, Synthetic / Q000737:chemistry*; D017550:Spectroscopy, Fourier Transform Infrared
D003486:Cyanides; D009942:Organometallic Compounds; D012117:Resins, Synthetic; D011092:Polyethylene Glycols; D007501:Iron; D006864:Hydrogenase