Abstract:
The CuA site of cytochromec oxidase is a redox hub that participates in rapid electron transfer at low driving forces with two redox cofactors in nearly perpendicular orientations. Spectroscopic and electrochemical characterizations performed on first and second-sphere mutants have allowed us to experimentally detect the reversible switching between two alternative electronic states that confer different directionalities to the redox reaction. Specifically, the M160H variant of a native CuA shows a reversible pH transition that allows to functionally probe both states in the same protein species. Alternation between states exerts a dramatic impact on the kinetic redox parameters, thereby suggesting this effect as the mechanism underlying the efficiency and directionality of CuA electron transfer invivo. These findings may also prove useful for the development of molecular electronics. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Registro:
Documento: |
Artículo
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Título: | Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in CuA Sites of Cytochrome c Oxidase |
Autor: | Zitare, U.; Alvarez-Paggi, D.; Morgada, M.N.; Abriata, L.A.; Vila, A.J.; Murgida, D.H. |
Filiación: | Instituto de Química Física de Los Materiales, Medio Ambiente y Ener., Depto. de Quim. Inorg., Analitica y Quim. Fis., Fac. de Cie. Exact. y Nat., Univ. de Buenos Aires and CONICET, Argentina Instituto de Biología Molecular y Celular de Rosario (IBR), Depto. de Quim. Biol., Fac. de Cie. Bioquimicas y Farmaceuticas, Univ. Nac. de Rosario and CONICET, Argentina
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Palabras clave: | cytochromec oxidase; electrochemistry; electron transfer; electronic structures; enzymes; Electrochemistry; Electron transitions; Electronic structure; Enzymes; Molecular orbitals; Redox reactions; Cytochrome c oxidase; Electrochemical characterizations; Electron transfer; Electron transfer pathways; Perpendicular orientation; Protein species; Redox cofactors; Reversible switching; Electrons; copper; cytochrome b; cytochrome ba3; cytochrome c oxidase; chemistry; electron; electron transport; enzymology; oxidation reduction reaction; Thermus thermophilus; Copper; Cytochrome b Group; Electron Transport; Electron Transport Complex IV; Electrons; Oxidation-Reduction; Thermus thermophilus |
Año: | 2015
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Volumen: | 54
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Número: | 33
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Página de inicio: | 9555
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Página de fin: | 9559
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DOI: |
http://dx.doi.org/10.1002/anie.201504188 |
Título revista: | Angewandte Chemie - International Edition
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Título revista abreviado: | Angew. Chem. Int. Ed.
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ISSN: | 14337851
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CODEN: | ACIEF
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CAS: | copper, 15158-11-9, 7440-50-8; cytochrome b, 9035-37-4; cytochrome c oxidase, 72841-18-0, 9001-16-5; Copper; Cytochrome b Group; cytochrome ba3; Electron Transport Complex IV
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Registro: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14337851_v54_n33_p9555_Zitare |
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Citas:
---------- APA ----------
Zitare, U., Alvarez-Paggi, D., Morgada, M.N., Abriata, L.A., Vila, A.J. & Murgida, D.H.
(2015)
. Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in CuA Sites of Cytochrome c Oxidase. Angewandte Chemie - International Edition, 54(33), 9555-9559.
http://dx.doi.org/10.1002/anie.201504188---------- CHICAGO ----------
Zitare, U., Alvarez-Paggi, D., Morgada, M.N., Abriata, L.A., Vila, A.J., Murgida, D.H.
"Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in CuA Sites of Cytochrome c Oxidase"
. Angewandte Chemie - International Edition 54, no. 33
(2015) : 9555-9559.
http://dx.doi.org/10.1002/anie.201504188---------- MLA ----------
Zitare, U., Alvarez-Paggi, D., Morgada, M.N., Abriata, L.A., Vila, A.J., Murgida, D.H.
"Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in CuA Sites of Cytochrome c Oxidase"
. Angewandte Chemie - International Edition, vol. 54, no. 33, 2015, pp. 9555-9559.
http://dx.doi.org/10.1002/anie.201504188---------- VANCOUVER ----------
Zitare, U., Alvarez-Paggi, D., Morgada, M.N., Abriata, L.A., Vila, A.J., Murgida, D.H. Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in CuA Sites of Cytochrome c Oxidase. Angew. Chem. Int. Ed. 2015;54(33):9555-9559.
http://dx.doi.org/10.1002/anie.201504188