Cargando…
Identifying conformational changes with site-directed spin labeling reveals that the GTPase domain of HydF is a molecular switch
[FeFe]-hydrogenases catalyse the reduction of protons to hydrogen at a complex 2Fe[4Fe4S] center called H-cluster. The assembly of this active site is a multistep process involving three proteins, HydE, HydF and HydG. According to the current models, HydF has the key double role of scaffold, upon wh...
Autores principales: | Galazzo, Laura, Maso, Lorenzo, De Rosa, Edith, Bortolus, Marco, Doni, Davide, Acquasaliente, Laura, De Filippis, Vincenzo, Costantini, Paola, Carbonera, Donatella |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5431965/ https://www.ncbi.nlm.nih.gov/pubmed/28490758 http://dx.doi.org/10.1038/s41598-017-01886-y |
Ejemplares similares
-
Overview of the Maturation Machinery of the H-Cluster of [FeFe]-Hydrogenases with a Focus on HydF
por: Bortolus, Marco, et al.
Publicado: (2018) -
Biosynthesis of the catalytic H-cluster of [FeFe] hydrogenase: the roles of the Fe–S maturase proteins HydE, HydF, and HydG
por: Britt, R. David, et al.
Publicado: (2020) -
Monitoring H-cluster assembly using a semi-synthetic HydF protein
por: Németh, Brigitta, et al.
Publicado: (2019) -
The maturase HydF enables [FeFe] hydrogenase assembly via transient, cofactor-dependent interactions
por: Németh, Brigitta, et al.
Publicado: (2020) -
Electron Spin Relaxation and Biochemical Characterization
of the Hydrogenase Maturase HydF: Insights into [2Fe-2S] and [4Fe-4S]
Cluster Communication and Hydrogenase Activation
por: Shepard, Eric M., et al.
Publicado: (2017)