Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 55, Issue 29, Pages 8396-8400Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201511896
Keywords
chalcogenide exchange; H-2 production; H-clusters; hydrogenases; selenium
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Funding
- Deutsche Forschungsgemeinschaft (DFG) [EXC1069]
- Volkswagen Foundation (LigH2t)
- EU
- Fonds of the Chemical Industry (Liebig grant)
- Deutsche Forschungsgemeinschaft [AP242/2-1]
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The [FeFe]-hydrogenase HYDA1 from Chlamydomonas reinhardtii is particularly amenable to biochemical and biophysical characterization because the H-cluster in the active site is the only inorganic cofactor present. Herein, we present the complete chemical incorporation of the H-cluster into the HYDA1-apoprotein scaffold and, furthermore, the successful replacement of sulfur in the native [4Fe(H)] cluster with selenium. The crystal structure of the reconstituted pre-mature HYDA1-[4Fe4Se](H) protein was determined, and a catalytically intact artificial H-cluster variant was generated upon in vitro maturation. Full hydrogen evolution activity as well as native-like composition and behavior of the redesigned enzyme were verified through kinetic assays, FTIR spectroscopy, and X-ray structure analysis. These findings reveal that even a bioinorganic active site with exceptional complexity can exhibit a surprising level of compositional plasticity.
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