Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 60, Issue 24, Pages 13350-13357Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.202100443
Keywords
biomimetics; hydrogen activation; hydrogenase; manganese; metal– ligand cooperation
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Funding
- Swiss National Science Foundation
- European Union Marie Sklodowska-Curie Individual Fellowships [794000]
- Max Planck Society
- Deutsche Forschungsgemeinschaft [SH 87/1-1]
- China Scholarship Council (CSC)
- Projekt DEAL
- EPFL
- Marie Curie Actions (MSCA) [794000] Funding Source: Marie Curie Actions (MSCA)
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The study discusses the reconstitution of [Mn]-hydrogenases using Mn-I complexes, highlighting the importance of internal base or pro-base in catalysis. The results confirm the essential role of metal-ligand cooperation for H-2 activation and indicate differences in the mode of cooperation between active [Mn]-hydrogenases and native [Fe]-hydrogenase. This work demonstrates the possibility of reconstituting active artificial hydrogenases using synthetic complexes.
The reconstitution of [Mn]-hydrogenases using a series of Mn-I complexes is described. These complexes are designed to have an internal base or pro-base that may participate in metal-ligand cooperative catalysis or have no internal base or pro-base. Only Mn-I complexes with an internal base or pro-base are active for H-2 activation; only [Mn]-hydrogenases incorporating such complexes are active for hydrogenase reactions. These results confirm the essential role of metal-ligand cooperation for H-2 activation by the Mn-I complexes alone and by [Mn]-hydrogenases. Owing to the nature and position of the internal base or pro-base, the mode of metal-ligand cooperation in two active [Mn]-hydrogenases is different from that of the native [Fe]-hydrogenase. One [Mn]-hydrogenase has the highest specific activity of semi-synthetic [Mn]- and [Fe]-hydrogenases. This work demonstrates reconstitution of active artificial hydrogenases using synthetic complexes differing greatly from the native active site.
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