- 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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Acyl and CO Ligands in the (Fe)‐Hydrogenase Cofactor Scramble upon Photolysis ; day:29 ; month:12 ; year:2023 ; extent:7
Angewandte Chemie ; (29.12.2023) (gesamt 7)
- Creator
- DOI
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10.1002/ange.202316478
- URN
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urn:nbn:de:101:1-2023123014065503088044
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:20 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Schaupp, Sebastian
- Arriaza‐Gallardo, Francisco J.
- Paczia, Nicole
- Ataka, Kenichi
- Shima, Seigo
Other Objects (12)
Acyl and CO Ligands in the (Fe)‐Hydrogenase Cofactor Scramble upon Photolysis
(Fe)‐Hydrogenase, Cofactor Biosynthesis and Engineering
In Vitro Biosynthesis of the FeGP Cofactor of the [Fe]-Hydrogenase
In Vitro Biosynthesis of the (Fe)‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors
In Vitro Biosynthesis of the (Fe)‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors
Identification and characterization of two radical SAM enzymes involved in biosynthesis of the [Fe]-hydrogenase cofactor
Cofactor composition and function of a H2-sensing regulatory hydrogenase as revealed by Mossbauer and EPR spectroscopy
Biocatalytic cofactor regeneration for CO2 reduction: Integration of a hydrogenase and a formate dehydrogenase in H2-driven systems
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the (Fe)‐Hydrogenase Cofactor
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the (Fe)‐Hydrogenase Cofactor
HONO measurement by differential photolysis
A membrane‐bound [NiFe]‐hydrogenase large subunit precursor whose C‐terminal extension is not essential for cofactor incorporation but guarantees optimal maturation
Acyl and CO Ligands in the (Fe)‐Hydrogenase Cofactor Scramble upon Photolysis
(Fe)‐Hydrogenase, Cofactor Biosynthesis and Engineering
In Vitro Biosynthesis of the FeGP Cofactor of the [Fe]-Hydrogenase
In Vitro Biosynthesis of the (Fe)‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors
In Vitro Biosynthesis of the (Fe)‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors
Identification and characterization of two radical SAM enzymes involved in biosynthesis of the [Fe]-hydrogenase cofactor
Cofactor composition and function of a H2-sensing regulatory hydrogenase as revealed by Mossbauer and EPR spectroscopy
Biocatalytic cofactor regeneration for CO2 reduction: Integration of a hydrogenase and a formate dehydrogenase in H2-driven systems
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the (Fe)‐Hydrogenase Cofactor
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the (Fe)‐Hydrogenase Cofactor
HONO measurement by differential photolysis
A membrane‐bound [NiFe]‐hydrogenase large subunit precursor whose C‐terminal extension is not essential for cofactor incorporation but guarantees optimal maturation
Acyl and CO Ligands in the (Fe)‐Hydrogenase Cofactor Scramble upon Photolysis
(Fe)‐Hydrogenase, Cofactor Biosynthesis and Engineering
In Vitro Biosynthesis of the FeGP Cofactor of the [Fe]-Hydrogenase
In Vitro Biosynthesis of the (Fe)‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors
In Vitro Biosynthesis of the (Fe)‐Hydrogenase Cofactor Verifies the Proposed Biosynthetic Precursors
Identification and characterization of two radical SAM enzymes involved in biosynthesis of the [Fe]-hydrogenase cofactor
Cofactor composition and function of a H2-sensing regulatory hydrogenase as revealed by Mossbauer and EPR spectroscopy
Biocatalytic cofactor regeneration for CO2 reduction: Integration of a hydrogenase and a formate dehydrogenase in H2-driven systems
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the (Fe)‐Hydrogenase Cofactor
The Function of Two Radical‐SAM Enzymes, HcgA and HcgG, in the Biosynthesis of the (Fe)‐Hydrogenase Cofactor
HONO measurement by differential photolysis