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InVivo EPR Characterization of Semi-Synthetic [FeFe] Hydrogenases
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- Meszaros, Livia S. (author)
- Uppsala universitet,Molekylär biomimetik
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- Nemeth, Brigitta (author)
- Uppsala universitet,Molekylär biomimetik
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- Esmieu, Charlène (author)
- Uppsala universitet,Molekylär biomimetik
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- (creator_code:org_t)
- 2018-02-06
- 2018
- English.
- In: Angewandte Chemie International Edition. - : WILEY-V C H VERLAG GMBH. - 1433-7851 .- 1521-3773. ; 57:10, s. 2596-2599
- Journal article (peer-reviewed)
Abstract
Subject headings
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- EPR spectroscopy reveals the formation of two different semi-synthetic hydrogenases invivo. [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 invivo, 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 invivo conditions.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- [FeFe] hydrogenase
- artificial enzymes
- EPR spectroscopy
- metalloenzymes
Publication and Content Type
- ref (subject category)
- art (subject category)
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