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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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

id	todo:paper_13597345_v49_n47_p5381_AlvarezPaggi
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spelling	todo:paper_13597345_v49_n47_p5381_AlvarezPaggi2023-10-03T16:10:42Z Native CuA redox sites are largely resilient to pH variations within a physiological range Alvarez-Paggi, D. Abriata, L.A. Murgida, D.H. Vila, A.J. 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 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. Fil:Alvarez-Paggi, D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_13597345_v49_n47_p5381_AlvarezPaggi
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	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
spellingShingle	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 Alvarez-Paggi, D. Abriata, L.A. Murgida, D.H. Vila, A.J. Native CuA redox sites are largely resilient to pH variations within a physiological range
topic_facet	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
description	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.
format	JOUR
author	Alvarez-Paggi, D. Abriata, L.A. Murgida, D.H. Vila, A.J.
author_facet	Alvarez-Paggi, D. Abriata, L.A. Murgida, D.H. Vila, A.J.
author_sort	Alvarez-Paggi, D.
title	Native CuA redox sites are largely resilient to pH variations within a physiological range
title_short	Native CuA redox sites are largely resilient to pH variations within a physiological range
title_full	Native CuA redox sites are largely resilient to pH variations within a physiological range
title_fullStr	Native CuA redox sites are largely resilient to pH variations within a physiological range
title_full_unstemmed	Native CuA redox sites are largely resilient to pH variations within a physiological range
title_sort	native cua redox sites are largely resilient to ph variations within a physiological range
url	http://hdl.handle.net/20.500.12110/paper_13597345_v49_n47_p5381_AlvarezPaggi
work_keys_str_mv	AT alvarezpaggid nativecuaredoxsitesarelargelyresilienttophvariationswithinaphysiologicalrange AT abriatala nativecuaredoxsitesarelargelyresilienttophvariationswithinaphysiologicalrange AT murgidadh nativecuaredoxsitesarelargelyresilienttophvariationswithinaphysiologicalrange AT vilaaj nativecuaredoxsitesarelargelyresilienttophvariationswithinaphysiologicalrange
_version_	1807317790392057856

Native CuA redox sites are largely resilient to pH variations within a physiological range

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