3 years ago![Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to HredH+ Transition in [FeFe] Hydrogenase](/image/eyJ1cmkiOiJodHRwOi8vc3RhY2thZGVtaWMuaGVyb2t1YXBwLmNvbS9pbWFnZT9pbWFnZV9pZD0xOTg2MSIsImZvcm1hdCI6IndlYnAiLCJxdWFsaXR5IjoxMDAsIndpZHRoIjo1MTIsIm5vQ2FjaGUiOnRydWV9.webp)
Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to HredH+ Transition in [FeFe] Hydrogenase
![Activation Thermodynamics and H/D Kinetic Isotope Effect of the Hox to HredH+ Transition in [FeFe] Hydrogenase](/image/eyJ1cmkiOiJodHRwOi8vc3RhY2thZGVtaWMuaGVyb2t1YXBwLmNvbS9pbWFnZT9pbWFnZV9pZD0xOTg2MSIsImZvcm1hdCI6IndlYnAiLCJxdWFsaXR5IjoxMDAsIndpZHRoIjo1MTIsIm5vQ2FjaGUiOnRydWV9.webp)
Carolyn E. Lubner, Molly B. Wilker, Michael W. Ratzloff, Gordana Dukovic, Katherine A. Brown, Hayden Hamby, Paul W. King, David W. Mulder
Molecular complexes between CdSe nanocrystals and Clostridium acetobutylicum [FeFe] hydrogenase I (CaI) enabled light-driven control of electron transfer for spectroscopic detection of redox intermediates during catalytic proton reduction. Here we address the route of electron transfer from CdSe→CaI and activation thermodynamics of the initial step of proton reduction in CaI. The electron paramagnetic spectroscopy of illuminated CdSe:CaI showed how the CaI accessory FeS cluster chain (F-clusters) functions in electron transfer with CdSe. The Hox→HredH+ reduction step measured by Fourier-transform infrared spectroscopy showed an enthalpy of activation of 19 kJ mol–1 and a ∼2.5-fold kinetic isotope effect. Overall, these results support electron injection from CdSe into CaI involving F-clusters, and that the Hox→HredH+ step of catalytic proton reduction in CaI proceeds by a proton-dependent process.
Publisher URL: http://dx.doi.org/10.1021/jacs.7b04216
DOI: 10.1021/jacs.7b04216
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