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Ilina_et_al-2019-Angewandte_Chemie_International_Edition
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Journal | Angewandte Chemie - International Edition |
---|---|
Date | Submitted - 3 Jul 2019 |
Date | Accepted/In press - 7 Oct 2019 |
Date | E-pub ahead of print (current) - 25 Oct 2019 |
Number of pages | 6 |
Early online date | 25/10/19 |
Original language | English |
[NiFe] hydrogenases are complex model enzymes for the reversible cleavage of dihydrogen (H2). However, structural determinants of efficient H2 binding to their [NiFe] active site are not properly understood. Here, we present crystallographic and vibrational-spectroscopic insights into the unexplored structure of the H2-binding [NiFe] intermediate. Using an F420-reducing [NiFe]-hydrogenase from Methanosarcina barkeri as a model enzyme, we show that the protein backbone provides a strained chelating scaffold that tunes the [NiFe] active site for efficient H2 binding and conversion. The protein matrix also directs H2 diffusion to the [NiFe] site via two gas channels and allows the distribution of electrons between functional protomers through a subunit-bridging FeS cluster. Our findings emphasize the relevance of an atypical Ni coordination, thereby providing a blueprint for the design of bio-inspired H2-conversion catalysts.
© 2019 The Authors.
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