A safety cap protects hydrogenase from oxygen attack
[FeFe]-hydrogenases catalyze the conversion of protons and electrons to molecular hydrogen, but upon exposure to oxygen, their catalytic cofactor is irreversibly inactivated. Here, the authors determine the crystal structure of hydrogenase CbA5H and identify a cysteine residue, which acts as a safet...
Guardado en:
Autores principales: | Martin Winkler, Jifu Duan, Andreas Rutz, Christina Felbek, Lisa Scholtysek, Oliver Lampret, Jan Jaenecke, Ulf-Peter Apfel, Gianfranco Gilardi, Francesca Valetti, Vincent Fourmond, Eckhard Hofmann, Christophe Léger, Thomas Happe |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2021
|
Materias: | |
Acceso en línea: | https://doaj.org/article/9c9745d6547b4e9c8c0781318c4c1e61 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases
por: Martin Winkler, et al.
Publicado: (2017) -
Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
por: Jifu Duan, et al.
Publicado: (2018) -
The influence of oxygen on [NiFe]-hydrogenase cofactor biosynthesis and how ligation of carbon monoxide precedes cyanation.
por: Sven T Stripp, et al.
Publicado: (2014) -
Evolutionary and biotechnological implications of robust hydrogenase activity in halophilic strains of Tetraselmis.
por: Sarah D'Adamo, et al.
Publicado: (2014) -
Suppressing hydrogen peroxide generation to achieve oxygen-insensitivity of a [NiFe] hydrogenase in redox active films
por: Huaiguang Li, et al.
Publicado: (2020)