Native CuA redox sites are largely resilient to pH variations within a physiological range
Previous studies on engineered CuA centres have shown that one of the histidine ligands is protonated and dissociated from the metal site at physiological pH values, thus suggesting a role in regulating proton-coupled electron transfer of cytochrome c oxidases in vivo. Here we report that for native...
Guardado en:
Autores principales: | Alvarez-Paggi, D., Abriata, L.A., Murgida, D.H., Vila, A.J. |
---|---|
Formato: | JOUR |
Materias: | |
Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_13597345_v49_n47_p5381_AlvarezPaggi |
Aporte de: |
Ejemplares similares
-
Native CuA redox sites are largely resilient to pH variations within a physiological range
por: Alvarez Paggi, Damian Jorge, et al.
Publicado: (2013) -
The met axial ligand determines the redox potential in CuA sites
por: Murgida, Daniel Horacio
Publicado: (2007) -
The met axial ligand determines the redox potential in CuA sites
por: Ledesma, G.N., et al. -
CuA-based chimeric T1 copper sites allow for
independent modulation of reorganization energy
and reduction potential
por: Szuster, Jonathan, et al.
Publicado: (2021) -
Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase
por: Zitare, U., et al.