title: Resonance Raman spectroscopy on [NiFe] hydrogenase provides structural insights into catalytic intermediates and reactions.
abstract: [NiFe] hydrogenases catalyze the reversible cleavage of hydrogen and, thus, represent model systems for the investigation and exploitation of emission-free energy conversion processes. Valuable information on the underlying molecular mechanisms can be obtained by spectroscopic techniques that monitor individual catalytic intermediates. Here, we employed resonance Raman spectroscopy and extended it to the entire binuclear active site of an oxygen-tolerant [NiFe] hydrogenase by probing the metal-ligand modes of both the Fe and, for the first time, the Ni ion. Supported by theoretical methods, this approach allowed for monitoring H-transfer from the active site and revealed novel insights into the so far unknown structure and electronic configuration of the hydrogen-binding intermediate of the catalytic cycle, thereby providing key information about catalytic intermediates and reactions of biological hydrogen activation.
authors: Institut für Chemie, Sekr. PC14, Technische Universität Berlin , Strasse des 17. Juni 135, D-10623 Berlin, Germany.
authors: Marius
authors: M
authors: Horch
authors: Janna
authors: J
authors: Schoknecht
authors: Maria Andrea
authors: MA
authors: Mroginski
authors: Oliver
authors: O
authors: Lenz
authors: Peter
authors: P
authors: Hildebrandt
authors: Ingo
authors: I
authors: Zebger
mesh_terms: D002384:Catalysis; D020134:Catalytic Domain; D006860:Hydrogen Bonding; D006864:Hydrogenase / Q000737:chemistry*; D008958:Models, Molecular; D008968:Molecular Conformation; D013059:Spectrum Analysis, Raman
chemical_list: C043296:nickel-iron hydrogenase; D006864:Hydrogenase