An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O₂-Tolerant Hydrogenase

To 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.

Subjects

enzyme models

IR spectroscopy

resonance Raman spectroscopy

spectroscopic models

[NiFe] hydrogenases

DDC Class

620: Ingenieurwissenschaften

Options

An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O₂-Tolerant Hydrogenase