Alternative ground states enable pathway switching in biological electron transfer
Electron transfer is the simplest chemical reaction and constitutes the basis of a large variety of biological processes, such as photosynthesis and cellular respiration. Nature has evolved specific proteins and cofactors for these functions. The mechanisms optimizing biological electron transfer ha...
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2012
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v109_n43_p17348_Abriata http://hdl.handle.net/20.500.12110/paper_00278424_v109_n43_p17348_Abriata |
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paper:paper_00278424_v109_n43_p17348_Abriata2023-06-08T14:54:27Z Alternative ground states enable pathway switching in biological electron transfer Cytochrome oxidase Invisible states NMR Paramagnetic proteins Spectroscopy copper proton article electrochemistry electron transport energy transfer membrane potential nonhuman priority journal protein protein interaction protein transport signal transduction spectroscopy Thermus thermophilus Electron Transport Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction Thermus thermophilus X-Ray Absorption Spectroscopy Electron transfer is the simplest chemical reaction and constitutes the basis of a large variety of biological processes, such as photosynthesis and cellular respiration. Nature has evolved specific proteins and cofactors for these functions. The mechanisms optimizing biological electron transfer have been matter of intense debate, such as the role of the protein milieu between donor and acceptor sites. Here we propose a mechanism regulating long-range electron transfer in proteins. Specifically, we report a spectroscopic, electrochemical, and theoretical study on WT and single-mutant CuA redox centers from Thermus thermophilus, which shows that thermal fluctuations may populate two alternative ground-state electronic wave functions optimized for electron entry and exit, respectively, through two different and nearly perpendicular pathways. These findings suggest a unique role for alternative or "invisible" electronic ground states in directional electron transfer. Moreover, it is shown that this energy gap and, therefore, the equilibrium between ground states can be fine-tuned by minor perturbations, suggesting alternative ways through which protein-protein interactions and membrane potential may optimize and regulate electron-proton energy transduction. 2012 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v109_n43_p17348_Abriata http://hdl.handle.net/20.500.12110/paper_00278424_v109_n43_p17348_Abriata |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Cytochrome oxidase Invisible states NMR Paramagnetic proteins Spectroscopy copper proton article electrochemistry electron transport energy transfer membrane potential nonhuman priority journal protein protein interaction protein transport signal transduction spectroscopy Thermus thermophilus Electron Transport Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction Thermus thermophilus X-Ray Absorption Spectroscopy |
| spellingShingle |
Cytochrome oxidase Invisible states NMR Paramagnetic proteins Spectroscopy copper proton article electrochemistry electron transport energy transfer membrane potential nonhuman priority journal protein protein interaction protein transport signal transduction spectroscopy Thermus thermophilus Electron Transport Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction Thermus thermophilus X-Ray Absorption Spectroscopy Alternative ground states enable pathway switching in biological electron transfer |
| topic_facet |
Cytochrome oxidase Invisible states NMR Paramagnetic proteins Spectroscopy copper proton article electrochemistry electron transport energy transfer membrane potential nonhuman priority journal protein protein interaction protein transport signal transduction spectroscopy Thermus thermophilus Electron Transport Nuclear Magnetic Resonance, Biomolecular Oxidation-Reduction Thermus thermophilus X-Ray Absorption Spectroscopy |
| description |
Electron transfer is the simplest chemical reaction and constitutes the basis of a large variety of biological processes, such as photosynthesis and cellular respiration. Nature has evolved specific proteins and cofactors for these functions. The mechanisms optimizing biological electron transfer have been matter of intense debate, such as the role of the protein milieu between donor and acceptor sites. Here we propose a mechanism regulating long-range electron transfer in proteins. Specifically, we report a spectroscopic, electrochemical, and theoretical study on WT and single-mutant CuA redox centers from Thermus thermophilus, which shows that thermal fluctuations may populate two alternative ground-state electronic wave functions optimized for electron entry and exit, respectively, through two different and nearly perpendicular pathways. These findings suggest a unique role for alternative or "invisible" electronic ground states in directional electron transfer. Moreover, it is shown that this energy gap and, therefore, the equilibrium between ground states can be fine-tuned by minor perturbations, suggesting alternative ways through which protein-protein interactions and membrane potential may optimize and regulate electron-proton energy transduction. |
| title |
Alternative ground states enable pathway switching in biological electron transfer |
| title_short |
Alternative ground states enable pathway switching in biological electron transfer |
| title_full |
Alternative ground states enable pathway switching in biological electron transfer |
| title_fullStr |
Alternative ground states enable pathway switching in biological electron transfer |
| title_full_unstemmed |
Alternative ground states enable pathway switching in biological electron transfer |
| title_sort |
alternative ground states enable pathway switching in biological electron transfer |
| publishDate |
2012 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00278424_v109_n43_p17348_Abriata http://hdl.handle.net/20.500.12110/paper_00278424_v109_n43_p17348_Abriata |
| _version_ |
1768546197230845952 |