Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function

Manipulation of the partition function (Q) of the redox center CuA from cytochrome c oxidase is attained by tuning the accessibility of a low lying alternative electronic ground state and by perturbation of the electrostatic potential through point mutations, loop engineering and pH variation. We re...

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Autores principales:	Alvarez-Paggi, D., Zitare, U.A., Szuster, J., Morgada, M.N., Leguto, A.J., Vila, A.J., Murgida, D.H.
Formato:	JOUR
Materias:	Ground state Redox reactions Axial ligand Cytochrome c oxidase Electronic ground state Electrostatic potentials Partition functions Point mutations Redox centers Redox potentials Tuning Article conformational transition electric activity enthalpy entropy hydrophobicity oxidation reduction potential oxidation reduction state partition coefficient pH quantum mechanics temperature dependence thermodynamics chemical phenomena chemistry electron metabolism oxidation reduction reaction static electricity copper cytochrome c oxidase ligand Copper Electron Transport Complex IV Electrons Entropy Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Ligands Oxidation-Reduction Static Electricity Thermodynamics
Acceso en línea:	http://hdl.handle.net/20.500.12110/paper_00027863_v139_n29_p9803_AlvarezPaggi
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	todo:paper_00027863_v139_n29_p9803_AlvarezPaggi
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spelling	todo:paper_00027863_v139_n29_p9803_AlvarezPaggi2023-10-03T13:54:29Z Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function Alvarez-Paggi, D. Zitare, U.A. Szuster, J. Morgada, M.N. Leguto, A.J. Vila, A.J. Murgida, D.H. Ground state Redox reactions Axial ligand Cytochrome c oxidase Electronic ground state Electrostatic potentials Partition functions Point mutations Redox centers Redox potentials Tuning Article conformational transition electric activity enthalpy entropy hydrophobicity oxidation reduction potential oxidation reduction state partition coefficient pH quantum mechanics temperature dependence thermodynamics chemical phenomena chemistry electron entropy metabolism oxidation reduction reaction static electricity thermodynamics copper cytochrome c oxidase ligand Copper Electron Transport Complex IV Electrons Entropy Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Ligands Oxidation-Reduction Static Electricity Thermodynamics Manipulation of the partition function (Q) of the redox center CuA from cytochrome c oxidase is attained by tuning the accessibility of a low lying alternative electronic ground state and by perturbation of the electrostatic potential through point mutations, loop engineering and pH variation. We report clear correlations of the entropic and enthalpic contributions to redox potentials with Q and with the identity and hydrophobicity of the weak axial ligand, respectively. © 2017 American Chemical Society. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00027863_v139_n29_p9803_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	Ground state Redox reactions Axial ligand Cytochrome c oxidase Electronic ground state Electrostatic potentials Partition functions Point mutations Redox centers Redox potentials Tuning Article conformational transition electric activity enthalpy entropy hydrophobicity oxidation reduction potential oxidation reduction state partition coefficient pH quantum mechanics temperature dependence thermodynamics chemical phenomena chemistry electron entropy metabolism oxidation reduction reaction static electricity thermodynamics copper cytochrome c oxidase ligand Copper Electron Transport Complex IV Electrons Entropy Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Ligands Oxidation-Reduction Static Electricity Thermodynamics
spellingShingle	Ground state Redox reactions Axial ligand Cytochrome c oxidase Electronic ground state Electrostatic potentials Partition functions Point mutations Redox centers Redox potentials Tuning Article conformational transition electric activity enthalpy entropy hydrophobicity oxidation reduction potential oxidation reduction state partition coefficient pH quantum mechanics temperature dependence thermodynamics chemical phenomena chemistry electron entropy metabolism oxidation reduction reaction static electricity thermodynamics copper cytochrome c oxidase ligand Copper Electron Transport Complex IV Electrons Entropy Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Ligands Oxidation-Reduction Static Electricity Thermodynamics Alvarez-Paggi, D. Zitare, U.A. Szuster, J. Morgada, M.N. Leguto, A.J. Vila, A.J. Murgida, D.H. Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
topic_facet	Ground state Redox reactions Axial ligand Cytochrome c oxidase Electronic ground state Electrostatic potentials Partition functions Point mutations Redox centers Redox potentials Tuning Article conformational transition electric activity enthalpy entropy hydrophobicity oxidation reduction potential oxidation reduction state partition coefficient pH quantum mechanics temperature dependence thermodynamics chemical phenomena chemistry electron entropy metabolism oxidation reduction reaction static electricity thermodynamics copper cytochrome c oxidase ligand Copper Electron Transport Complex IV Electrons Entropy Hydrogen-Ion Concentration Hydrophobic and Hydrophilic Interactions Ligands Oxidation-Reduction Static Electricity Thermodynamics
description	Manipulation of the partition function (Q) of the redox center CuA from cytochrome c oxidase is attained by tuning the accessibility of a low lying alternative electronic ground state and by perturbation of the electrostatic potential through point mutations, loop engineering and pH variation. We report clear correlations of the entropic and enthalpic contributions to redox potentials with Q and with the identity and hydrophobicity of the weak axial ligand, respectively. © 2017 American Chemical Society.
format	JOUR
author	Alvarez-Paggi, D. Zitare, U.A. Szuster, J. Morgada, M.N. Leguto, A.J. Vila, A.J. Murgida, D.H.
author_facet	Alvarez-Paggi, D. Zitare, U.A. Szuster, J. Morgada, M.N. Leguto, A.J. Vila, A.J. Murgida, D.H.
author_sort	Alvarez-Paggi, D.
title	Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
title_short	Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
title_full	Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
title_fullStr	Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
title_full_unstemmed	Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function
title_sort	tuning of enthalpic/entropic parameters of a protein redox center through manipulation of the electronic partition function
url	http://hdl.handle.net/20.500.12110/paper_00027863_v139_n29_p9803_AlvarezPaggi
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Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function

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