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. Thi...

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2017-02, Vol.56 (8), p.2208-2211
Main Authors: Lindenmaier, Nils J., Wahlefeld, Stefan, Bill, Eckhard, Szilvási, Tibor, Eberle, Christopher, Yao, Shenglai, Hildebrandt, Peter, Horch, Marius, Zebger, Ingo, Driess, Matthias
Format: Article
Language:English
Subjects:
[NiFe] hydrogenases
Biomimetics
enzyme models
Enzymes
Hydrogenase
Intermediates
Intermetallic compounds
IR spectroscopy
Iron compounds
NAD
Nickel compounds
Oxygenation
resonance Raman spectroscopy
spectroscopic models
Spectroscopy
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Summary: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. Vibrant insight: The first S‐oxygenated [NiFe] complex is a structural and vibrational spectroscopic model for the S‐oxygenated active site of the NAD+‐reducing [NiFe] hydrogenase from Ralstonia eutropha. A combined spectroscopic and theoretical study reveals a highly polarized sulfenato moiety in the bioinspired model complex, thereby providing a key perspective for future investigations of this enzyme.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201611069