Accumulating the hydride state in the catalytic cycle of [FeFe]-hydrogenases
Of the four intermediates in the catalytic cycle of [FeFe]-hydrogenases, the hydride state still has eluded characterization. Here, the authors shift the reaction equilibrium for three hydrogenases and enrich the hydride-bound species, characterizing them using a real-time IR spectroscopic technique...
Guardado en:
Autores principales: | Martin Winkler, Moritz Senger, Jifu Duan, Julian Esselborn, Florian Wittkamp, Eckhard Hofmann, Ulf-Peter Apfel, Sven Timo Stripp, Thomas Happe |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/8b8423f5ac15415e844771a44e6de8f5 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Crystallographic and spectroscopic assignment of the proton transfer pathway in [FeFe]-hydrogenases
por: Jifu Duan, et al.
Publicado: (2018) -
A cell-free microtiter plate screen for improved [FeFe] hydrogenases.
por: James A Stapleton, et al.
Publicado: (2010) -
A safety cap protects hydrogenase from oxygen attack
por: Martin Winkler, et al.
Publicado: (2021) -
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) -
Analyses of the large subunit histidine-rich motif expose an alternative proton transfer pathway in [NiFe] hydrogenases.
por: Emma Szőri-Dorogházi, et al.
Publicado: (2012)