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...
Guardado en:
| Autores principales: | , , , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00027863_v139_n29_p9803_AlvarezPaggi |
| Aporte de: |
| id |
todo:paper_00027863_v139_n29_p9803_AlvarezPaggi |
|---|---|
| record_format |
dspace |
| 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 |
| work_keys_str_mv |
AT alvarezpaggid tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction AT zitareua tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction AT szusterj tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction AT morgadamn tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction AT legutoaj tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction AT vilaaj tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction AT murgidadh tuningofenthalpicentropicparametersofaproteinredoxcenterthroughmanipulationoftheelectronicpartitionfunction |
| _version_ |
1807318513983946752 |