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

Nils J. Lindenmaier, Stefan Wahlefeld, Eckhard Bill, Tibor Szilvási, Christopher Eberle, Shenglai Yao, Peter Hildebrandt, Marius Horch*, Ingo Zebger, Matthias Driess

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)2208-2211
Number of pages4
JournalAngewandte Chemie - International Edition
Issue number8
Publication statusPublished - 1 Jan 2017


  • enzyme models
  • IR spectroscopy
  • resonance Raman spectroscopy
  • spectroscopic models
  • [NiFe] hydrogenases

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