Protonation of a subsite analogue of [FeFe]-hydrogenase: mechanism of a deceptively simple reaction revealed by time-resolved IR spectroscopy.
We provide the first detailed time-resolved mechanistic information on the protonation of a model of the subsite of [FeFe]-hydrogenase, [Fe2(mu-pdt)(CO)4(PMe3)2]; the deceptively simple stoichiometric reaction is shown to be limited by the rate of protonation of the basal-apical isomer followed by its rearrangement to the transoid basal form.
Energy Materials Laboratory, School of Chemistry, University of East Anglia, Norwich, UK NR4 7TJ.
Joseph A
JA
Wright
Christopher J
CJ
Pickett
D006864:Hydrogenase / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry*; D007700:Kinetics; D009682:Magnetic Resonance Spectroscopy; D009942:Organometallic Compounds / Q000737:chemistry*; D010165:Palladium / Q000737:chemistry*; D011522:Protons; D013055:Spectrophotometry, Infrared; D013056:Spectrophotometry, Ultraviolet
D009942:Organometallic Compounds; D011522:Protons; D010165:Palladium; D007501:Iron; D006864:Hydrogenase