Abstract:
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.
Registro:
Documento: |
Artículo
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Título: | Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function |
Autor: | Alvarez-Paggi, D.; Zitare, U.A.; Szuster, J.; Morgada, M.N.; Leguto, A.J.; Vila, A.J.; Murgida, D.H. |
Filiación: | Instituto de Química Física de Los Materiales, Medio Ambiente y Energía, Departamento de Química Inorgánica, Analítica y Química Física, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, CONICET, Buenos Aires, 1428, Argentina Instituto de Biología Molecular y Celular de Rosario (IBR), Departamento de Química Biológica, Facultad de Ciencias Bioquímicas y Farmacéuticas, Universidad Nacional de Rosario, CONICET, Rosario, 2000, Argentina Instituto de Investigaciones Bioquimicas de Buenos Aires, FILCONICET, Argentina
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Palabras clave: | 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 |
Año: | 2017
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Volumen: | 139
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Número: | 29
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Página de inicio: | 9803
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Página de fin: | 9806
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DOI: |
http://dx.doi.org/10.1021/jacs.7b05199 |
Título revista: | Journal of the American Chemical Society
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Título revista abreviado: | J. Am. Chem. Soc.
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ISSN: | 00027863
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CODEN: | JACSA
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CAS: | copper, 15158-11-9, 7440-50-8; cytochrome c oxidase, 72841-18-0, 9001-16-5; Copper; Electron Transport Complex IV; Ligands
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00027863_v139_n29_p9803_AlvarezPaggi |
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Citas:
---------- APA ----------
Alvarez-Paggi, D., Zitare, U.A., Szuster, J., Morgada, M.N., Leguto, A.J., Vila, A.J. & Murgida, D.H.
(2017)
. Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function. Journal of the American Chemical Society, 139(29), 9803-9806.
http://dx.doi.org/10.1021/jacs.7b05199---------- CHICAGO ----------
Alvarez-Paggi, D., Zitare, U.A., Szuster, J., Morgada, M.N., Leguto, A.J., Vila, A.J., et al.
"Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function"
. Journal of the American Chemical Society 139, no. 29
(2017) : 9803-9806.
http://dx.doi.org/10.1021/jacs.7b05199---------- MLA ----------
Alvarez-Paggi, D., Zitare, U.A., Szuster, J., Morgada, M.N., Leguto, A.J., Vila, A.J., et al.
"Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function"
. Journal of the American Chemical Society, vol. 139, no. 29, 2017, pp. 9803-9806.
http://dx.doi.org/10.1021/jacs.7b05199---------- VANCOUVER ----------
Alvarez-Paggi, D., Zitare, U.A., Szuster, J., Morgada, M.N., Leguto, A.J., Vila, A.J., et al. Tuning of Enthalpic/Entropic Parameters of a Protein Redox Center through Manipulation of the Electronic Partition Function. J. Am. Chem. Soc. 2017;139(29):9803-9806.
http://dx.doi.org/10.1021/jacs.7b05199