In Vivo EPR Characterization of Semi‐Synthetic (FeFe) Hydrogenases
Abstract: EPR spectroscopy reveals the formation of two different semi‐synthetic hydrogenases in vivo. [FeFe] hydrogenases are metalloenzymes that catalyze the interconversion of molecular hydrogen and protons. The reaction is catalyzed by the H‐cluster, consisting of a canonical iron–sulfur cluster and an organometallic [2Fe] subsite. It was recently shown that the enzyme can be reconstituted with synthetic cofactors mimicking the composition of the [2Fe] subsite, resulting in semi‐synthetic hydrogenases. Herein, we employ EPR spectroscopy to monitor the formation of two such semi‐synthetic enzymes in whole cells. The study provides the first spectroscopic characterization of semi‐synthetic hydrogenases in vivo, and the observation of two different oxidized states of the H‐cluster under intracellular conditions. Moreover, these findings underscore how synthetic chemistry can be a powerful tool for manipulation and examination of the hydrogenase enzyme under in vivo conditions.
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
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Englisch
- Bibliographic citation
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In Vivo EPR Characterization of Semi‐Synthetic (FeFe) Hydrogenases ; volume:130 ; number:10 ; year:2018 ; pages:2626-2629 ; extent:4
Angewandte Chemie ; 130, Heft 10 (2018), 2626-2629 (gesamt 4)
- Creator
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Mészáros, Lívia S.
Németh, Brigitta
Esmieu, Charlène
Ceccaldi, Pierre
Berggren, Gustav
- DOI
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10.1002/ange.201710740
- URN
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urn:nbn:de:101:1-2022090819192657644214
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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15.08.2025, 7:28 AM CEST
Data provider
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Mészáros, Lívia S.
- Németh, Brigitta
- Esmieu, Charlène
- Ceccaldi, Pierre
- Berggren, Gustav
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