By the same authors

From the same journal

From the same journal

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

Research output: Contribution to journalArticlepeer-review

Full text download(s)

Published copy (DOI)


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


Publication details

JournalAngewandte Chemie - International Edition
DateSubmitted - 3 Jul 2019
DateAccepted/In press - 7 Oct 2019
DateE-pub ahead of print (current) - 25 Oct 2019
Number of pages6
Early online date25/10/19
Original languageEnglish


[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.

Bibliographical note

© 2019 The Authors.

    Research areas

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

Discover related content

Find related publications, people, projects, datasets and more using interactive charts.

View graph of relations