Lindenmaier, Nils JNils JLindenmaierWahlefeld, StefanStefanWahlefeldBill, EckhardEckhardBillSzilvási, TiborTiborSzilvásiEberle, ChristopherChristopherEberleYao, ShenglaiShenglaiYaoHildebrandt, PeterPeterHildebrandtHorch, MariusMariusHorchZebger, IngoIngoZebgerDriess, MatthiasMatthiasDriess2020-01-232020-01-232017-01-12Angewandte Chemie - International Edition 8 (56): 2208-2211 (2017-01-01)http://hdl.handle.net/11420/4491To understand the molecular details of O2-tolerant hydrogen cycling by a soluble NAD+-reducing [NiFe] hydrogenase, we herein present the first bioinspired heterobimetallic S-oxygenated [NiFe] complex as a structural and vibrational spectroscopic model for the oxygen-inhibited [NiFe] active site. This compound and its non-S-oxygenated congener were fully characterized, and their electronic structures were elucidated in a combined experimental and theoretical study with emphasis on the bridging sulfenato moiety. Based on the vibrational spectroscopic properties of these complexes, we also propose novel strategies for exploring S-oxygenated intermediates in hydrogenases and similar enzymes.1521-37732017822082211enzyme modelsIR spectroscopyresonance Raman spectroscopyspectroscopic models[NiFe] hydrogenasesIngenieurwissenschaftenJournal Article10.1002/anie.201611069Journal Article