New joint paper by Driess and Hildebrandt in Angewandte Chemie. 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.
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.
Original publication
An S-Oxygenated [NiFe] Complex Modelling Sulfenate Intermediates of an O2-Tolerant Hydrogenase
Nils J. Lindenmaier, Stefan Wahlefeld, Eckhard Bill, Tribor Szilvási, Christopher Eberle, Shenglai Yao, Peter Hildebrandt, Marius Horch, Ingo Zebger, Matthias Driess
Angew. Chem. Int. Ed. 2017
DOI: 10.1002/anie.201611069
or in Selected Research Highlights