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  Sensitivity-enhanced magnetic resonance reveals hydrogen intermediates during active [Fe]-hydrogenase catalysis

Kaltschnee, L., Pravdivtsev, A. N., Gehl, M., Huang, G., Stoychev, G. L., Riplinger, C., et al. (2023). Sensitivity-enhanced magnetic resonance reveals hydrogen intermediates during active [Fe]-hydrogenase catalysis. bioRxiv: the preprint server for biology, doi: 10.1101/2023.05.10.540199.

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Kaltschnee, Lukas1, Author
Pravdivtsev, Andrey N.1, Author
Gehl, Manuel2, Author                 
Huang, Gangfeng2, Author           
Stoychev, Georgi L.1, Author
Riplinger, Christoph1, Author
Keitel, Maximilian1, Author
Neese, Frank1, Author
Hövener, Jan-Bernd1, Author
Auer, Alexander A.1, Author
Griesinger, Christian1, Author
Shima, Seigo2, Author                 
Glöggler, Stefan1, Author
Affiliations:
1external, ou_persistent22              
2Department-Independent Research Group Microbial Protein Structure, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, ou_3266277              

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 Abstract: Molecular hydrogen (H2) is considered an eco-friendly future energy-carrier and an alternative to fossil fuel1 and thus, major efforts are directed towards identifying efficient and economical hydrogen catalysts.2,3 Efficient hydrogen catalysis is used by many microorganisms, some of them producing H2 from organic materials and others consuming it.4-6 To metabolize H2, these microorganisms use enzymes called hydrogenases.7,8 For the future development of efficient catalysts a detailed analysis of the catalytic mechanisms of such hydrogenases is required and existing analytical techniques could not provide a full understanding.9 Consequently, new analytical technologies are of utmost importance to unravel natures' blueprints for highly efficient hydrogen catalysts. Here, we introduce signal-enhanced or hyperpolarized, nuclear magnetic resonance (NMR) to study hydrogenases under turnover conditions. So far undiscovered hydrogen species of the catalytic cycle of [Fe]-hydrogenases, are revealed and thus, extend the knowledge regarding this class of enzymes. These findings pave new pathways for the exploration of novel hydrogen metabolisms in vivo. We furthermore envision that the results contribute to the rational design of future catalysts to solve energy challenges of our society.Competing Interest StatementThe authors have declared no competing interest.

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Language(s): eng - English
 Dates: 2023-01
 Publication Status: Issued
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 Rev. Type: No review
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Title: bioRxiv : the preprint server for biology
  Abbreviation : bioRxiv
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: doi: 10.1101/2023.05.10.540199 Start / End Page: - Identifier: ZDB: 2766415-6
CoNE: https://pure.mpg.de/cone/journals/resource/2766415-6