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X‐ray Crystallography and Vibrational Spectroscopy Reveal the Key Determinants of Biocatalytic Dihydrogen Cycling by [NiFe] Hydrogenases
Author(s) -
Ilina Yulia,
Lorent Christian,
Katz Sagie,
Jeoung JaeHun,
Shima Seigo,
Horch Marius,
Zebger Ingo,
Dobbek Holger
Publication year - 2019
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201908258
Subject(s) - hydrogenase , crystallography , active site , chemistry , catalysis , crystal structure , materials science , biochemistry
[NiFe] hydrogenases are complex model enzymes for the reversible cleavage of dihydrogen (H 2 ). However, structural determinants of efficient H 2 binding to their [NiFe] active site are not properly understood. Here, we present crystallographic and vibrational‐spectroscopic insights into the unexplored structure of the H 2 ‐binding [NiFe] intermediate. Using an F 420 ‐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 H 2 binding and conversion. The protein matrix also directs H 2 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 H 2 ‐conversion catalysts.