Model of the [FeFe] Hydrogenase Active Site with a Biologically Relevant Azadithiolate Bridge: A Spectroscopic and Theoretical Investigation

Convincing evidence for the presence of a nitrogen atom in the dithiolate bridge of the active site of native [FeFe] hydrogenases (B) is provided by a spectroscopic, electrochemical, and theoretical study of a well‐characterized structural mimic of the [FeFe] hydrogenase subcluster (picture: 14N mat...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2011-02, Vol.50 (6), p.1439-1443
Main Authors: Erdem, Özlen F, Schwartz, Lennart, Stein, Matthias, Silakov, Alexey, Kaur-Ghumaan, Sandeep, Huang, Ping, Ott, Sascha, Reijerse, Edward J, Lubitz, Wolfgang
Format: Article
Language:English
Subjects:
Aza Compounds - chemistry
Catalytic Domain
Chemistry
density functional calculations
Electrochemical Techniques
Electron Spin Resonance Spectroscopy
ENDOR spectroscopy
enzyme models
EPR spectroscopy
Hydrogenase - chemistry
Hydrogenase - metabolism
hydrogenases
Iron-Sulfur Proteins - chemistry
Iron-Sulfur Proteins - metabolism
Kemi
Models, Theoretical
NATURAL SCIENCES
NATURVETENSKAP
Spectroscopy, Fourier Transform Infrared
Sulfhydryl Compounds - chemistry
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Summary:Convincing evidence for the presence of a nitrogen atom in the dithiolate bridge of the active site of native [FeFe] hydrogenases (B) is provided by a spectroscopic, electrochemical, and theoretical study of a well‐characterized structural mimic of the [FeFe] hydrogenase subcluster (picture: 14N matched‐HYSCORE spectrum of the model compound A). This result should help to understand the mechanism of dihydrogen conversion and production.
ISSN:1433-7851
1521-3773
1521-3773
DOI:10.1002/anie.201006244