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, Damian Jorge, Murgida, Daniel Horacio
Publicado:	2013
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:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v49_n47_p5381_AlvarezPaggi 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	paper:paper_13597345_v49_n47_p5381_AlvarezPaggi
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spelling	paper:paper_13597345_v49_n47_p5381_AlvarezPaggi2023-06-08T16:11:28Z Native CuA redox sites are largely resilient to pH variations within a physiological range Alvarez Paggi, Damian Jorge Murgida, Daniel Horacio 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. 2013 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v49_n47_p5381_AlvarezPaggi 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, Damian Jorge Murgida, Daniel Horacio 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.
author	Alvarez Paggi, Damian Jorge Murgida, Daniel Horacio
author_facet	Alvarez Paggi, Damian Jorge Murgida, Daniel Horacio
author_sort	Alvarez Paggi, Damian Jorge
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
publishDate	2013
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_13597345_v49_n47_p5381_AlvarezPaggi http://hdl.handle.net/20.500.12110/paper_13597345_v49_n47_p5381_AlvarezPaggi
work_keys_str_mv	AT alvarezpaggidamianjorge nativecuaredoxsitesarelargelyresilienttophvariationswithinaphysiologicalrange AT murgidadanielhoracio nativecuaredoxsitesarelargelyresilienttophvariationswithinaphysiologicalrange
_version_	1768544463090614272

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

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