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...

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Detalles Bibliográficos
Autores principales: Alvarez-Paggi, D., Abriata, L.A., Murgida, D.H., Vila, A.J.
Formato: JOUR
Materias:
copper
metal
article
chemical structure
electron
excitation
oxidation reduction reaction
pH
physiology
proton transport
spectroscopy
Copper
Electrochemistry
Electron Transport Complex IV
Hydrogen-Ion Concentration
Oxidation-Reduction
Spectrum Analysis
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_13597345_v49_n47_p5381_AlvarezPaggi
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires
Descripción
Sumario: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 CuA such protonation does not take place at physiologically relevant pH values and, furthermore, no significant changes in the spectroscopic and redox properties of the metal site occur at low pH. © 2013 The Royal Society of Chemistry.

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