Cargando…
A site-differentiated [4Fe–4S] cluster controls electron transfer reactivity of Clostridium acetobutylicum [FeFe]-hydrogenase I
One of the many functions of reduction–oxidation (redox) cofactors is to mediate electron transfer in biological enzymes catalyzing redox-based chemical transformation reactions. There are numerous examples of enzymes that utilize redox cofactors to form electron transfer relays to connect catalytic...
Autores principales: | Lubner, Carolyn E., Artz, Jacob H., Mulder, David W., Oza, Aisha, Ward, Rachel J., Williams, S. Garrett, Jones, Anne K., Peters, John W., Smalyukh, Ivan I., Bharadwaj, Vivek S., King, Paul W. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Royal Society of Chemistry
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9019909/ https://www.ncbi.nlm.nih.gov/pubmed/35656134 http://dx.doi.org/10.1039/d1sc07120c |
Ejemplares similares
-
The Contribution of Proton-Donor pKa on Reactivity Profiles of [FeFe]-hydrogenases
por: Kisgeropoulos, Effie C., et al.
Publicado: (2022) -
Energetics for Proton Reduction in FeFe Hydrogenase
por: Siegbahn, Per E. M., et al.
Publicado: (2020) -
Inhibition of [FeFe]-hydrogenase by formaldehyde: proposed mechanism and reactivity of FeFe alkyl complexes
por: Zhang, Fanjun, et al.
Publicado: (2021) -
[NiFe], [FeFe], and [Fe] hydrogenase models from isomers
por: Ogo, Seiji, et al.
Publicado: (2020) -
Fantastic [FeFe]-Hydrogenases and Where to Find Them
por: Morra, Simone
Publicado: (2022)