Observation of the FeCN and FeCO Vibrations in the Active Site of [NiFe] Hydrogenase by Nuclear Resonance Vibrational Spectroscopy

Nuclear inelastic scattering of 57Fe labeled [NiFe] hydrogenase is shown to give information on different states of the enzyme. It was thus possible to detect and assign FeCO and FeCN bending and stretching vibrations of the active site outside the spectral range of the FeS cluster normal modes....

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Bibliographic Details
Published in:Angewandte Chemie International Edition 2013-01, Vol.52 (2), p.724-728
Main Authors: Kamali, Saeed, Wang, Hongxin, Mitra, Devrani, Ogata, Hideaki, Lubitz, Wolfgang, Manor, Brian C., Rauchfuss, Thomas B., Byrne, Deborah, Bonnefoy, Violaine, Jenney Jr, Francis E., Adams, Michael W. W., Yoda, Yoshitaka, Alp, Ercan, Zhao, Jiyong, Cramer, Stephen P.
Format: Article
Language:English
Subjects:
Bending
Catalytic Domain
Electron Spin Resonance Spectroscopy
FeS clusters
Hydrogenase
Hydrogenase - chemistry
Hydrogenase - metabolism
hydrogenases
Intermetallics
Iron compounds
Iron Compounds - chemistry
Models, Molecular
Nickel base alloys
Nickel compounds
NiFe acvite site
Oxidation-Reduction
Spectra
spectroscopic methods
Spectroscopy, Fourier Transform Infrared
Vibration
vibrational spectroscopy
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Summary:Nuclear inelastic scattering of 57Fe labeled [NiFe] hydrogenase is shown to give information on different states of the enzyme. It was thus possible to detect and assign FeCO and FeCN bending and stretching vibrations of the active site outside the spectral range of the FeS cluster normal modes.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201204616