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Updated: Jan 12, 2026
![Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase](/_next/image?url=https%3A%2F%2Fcloudfront.jove.com%2FCDNSource%2Fteasers%2F55858.jpg&w=3840&q=50)
Protein Film Infrared Electrochemistry Demonstrated for Study of H2 Oxidation by a [NiFe] Hydrogenase
Published on: December 4, 2017
NRVS Spectroscopy Resolves Distinct Bridging Hydride Intermediates in [NiFe]-Hydrogenase
Giorgio Caserta1, Konstantin Laun1, Jean-Pierre Oudsen1
1Institut für Chemie, Technische Universität Berlin, Straße des 17. Juni 135, 10623 Berlin, Germany.
Abstract:
The active-site iron of an H2-sensing [NiFe]-hydrogenase was selectively labeled with 57Fe, allowing the probing of all catalytic intermediates using synchrotron-based nuclear resonance vibrational spectroscopy. Diagnostic metal-hydride vibrations were detected for both the Nia-C and Nia-SR intermediates, with their assignments being confirmed through H/D isotope substitution and in situ hydride photolysis experiments. Interestingly, these Fe-hydride bands are separated by a large energy gap, reflecting distinct bonding interactions at the metal-hydride site. Despite these differences, vibrational analyses across all catalytically active species reveal a conserved structural rigidity of the [NiFe] center, which appears crucial for sustaining efficient and rapid electron transfer in [NiFe]-hydrogenases.
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