X-ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases

Yulia Ilina, Christian Lorent, Sagie Katz, Jae Hun Jeoung, Seigo Shima, Marius Horch*, Ingo Zebger, Holger Dobbek

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


[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.

Original languageEnglish
Number of pages6
JournalAngewandte Chemie - International Edition
Early online date25 Oct 2019
Publication statusE-pub ahead of print - 25 Oct 2019

Bibliographical note

© 2019 The Authors.


  • biocatalysis
  • crystal structure
  • hydrogen activation
  • vibrational spectroscopy
  • [NiFe] hydrogenase

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