Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase
The Cu<inf>A</inf> 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...
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todo:paper_14337851_v54_n33_p9555_Zitare2023-10-03T16:14:12Z Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase Zitare, U. Alvarez-Paggi, D. Morgada, M.N. Abriata, L.A. Vila, A.J. Murgida, D.H. 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 The Cu<inf>A</inf> 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 Cu<inf>A</inf> 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 Cu<inf>A</inf> electron transfer invivo. These findings may also prove useful for the development of molecular electronics. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_14337851_v54_n33_p9555_Zitare |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 |
| spellingShingle |
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 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 Cu<inf>A</inf> Sites of Cytochrome c Oxidase |
| topic_facet |
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 |
| description |
The Cu<inf>A</inf> 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 Cu<inf>A</inf> 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 Cu<inf>A</inf> electron transfer invivo. These findings may also prove useful for the development of molecular electronics. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim. |
| format |
JOUR |
| author |
Zitare, U. Alvarez-Paggi, D. Morgada, M.N. Abriata, L.A. Vila, A.J. Murgida, D.H. |
| author_facet |
Zitare, U. Alvarez-Paggi, D. Morgada, M.N. Abriata, L.A. Vila, A.J. Murgida, D.H. |
| author_sort |
Zitare, U. |
| title |
Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase |
| title_short |
Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase |
| title_full |
Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase |
| title_fullStr |
Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase |
| title_full_unstemmed |
Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase |
| title_sort |
reversible switching of redox-active molecular orbitals and electron transfer pathways in cu<inf>a</inf> sites of cytochrome c oxidase |
| url |
http://hdl.handle.net/20.500.12110/paper_14337851_v54_n33_p9555_Zitare |
| work_keys_str_mv |
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