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From the same journal

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

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Published copy (DOI)

Author(s)

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

Department/unit(s)

Publication details

JournalAngewandte Chemie - International Edition
DatePublished - 1 Jan 2017
Issue number8
Volume56
Number of pages4
Pages (from-to)2208-2211
Original languageEnglish

Abstract

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.

    Research areas

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

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