Reconstitution of respiratory complex I on a biomimetic membrane supported on gold electrodes
For the first time, respiratory complex I has been reconstituted on an electrode preserving its structure and activity. Respiratory complex I is a membrane-bound enzyme that has an essential function in cellular energy production. It couples NADH:quinone oxidoreduction to translocation of ions acros...
| Autores: | , , , , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2014 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/142779 |
| Acceso en línea: | http://hdl.handle.net/10261/142779 |
| Access Level: | acceso abierto |
| Palabra clave: | Infrared-absorption spectroscopy Nadh-Ubiquinone oxidoreductase Escherichia-coli Rhodothermus-marinus Lipid-membrane Cluster N2 Electrochemistry Oxidation Transport Bilayer Adenosinetriphosphate Atomic force microscopy Biomimetics Cell membranes Electrodes Gold Organic polymers Self assembled monolayers Electrochemical measurements Electrochemical potential Membrane-bound enzymes Mitochondrial membranes Proton translocation Respiratory complex Structure and activities Thiol self-assembled monolayers Gold compounds Artificial membranes Bacterial proteins Biomimetic materials Proton Reduced nicotinamide adenine dinucleotide dehydrogenase (ubiquinone) Thiol reagent Chemistry Electrode Electron transport Enzymology Isolation and purification Rhodothermus Electron Transport Complex I Membranes, Artificial Microscopy, Atomic Force Protons Sulfhydryl Reagents |
| Sumario: | For the first time, respiratory complex I has been reconstituted on an electrode preserving its structure and activity. Respiratory complex I is a membrane-bound enzyme that has an essential function in cellular energy production. It couples NADH:quinone oxidoreduction to translocation of ions across the cellular (in prokaryotes) or mitochondrial membranes. Therefore, complex I contributes to the establishment and maintenance of the transmembrane difference of electrochemical potential required for adenosine triphosphate synthesis, transport, and motility. Our new strategy has been applied for reconstituting the bacterial complex I from Rhodothermus marinus onto a biomimetic membrane supported on gold electrodes modified with a thiol self-assembled monolayer (SAM). Atomic force microscopy and faradaic impedance measurements give evidence of the biomimetic construction, whereas electrochemical measurements show its functionality. Both electron transfer and proton translocation by respiratory complex I were monitored, simulating in vivo conditions. © 2014 American Chemical Society. |
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