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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2015
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14337851_v54_n33_p9555_Zitare http://hdl.handle.net/20.500.12110/paper_14337851_v54_n33_p9555_Zitare |
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paper:paper_14337851_v54_n33_p9555_Zitare2023-06-08T16:14:20Z Reversible Switching of Redox-Active Molecular Orbitals and Electron Transfer Pathways in Cu<inf>A</inf> Sites of Cytochrome c Oxidase 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. 2015 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14337851_v54_n33_p9555_Zitare 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 |
| collection |
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 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. |
| 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 |
| publishDate |
2015 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_14337851_v54_n33_p9555_Zitare http://hdl.handle.net/20.500.12110/paper_14337851_v54_n33_p9555_Zitare |
| _version_ |
1768541812766539776 |