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Biomimetic Membranes for Multi-Redox Center Proteins

Austrian Institute of Technology GmbH, AIT, Donau-City-Str. 1, 1220 Vienna, Austria
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Author to whom correspondence should be addressed.
Academic Editor: Bernhard Schuster
Int. J. Mol. Sci. 2016, 17(3), 330; https://doi.org/10.3390/ijms17030330
Received: 7 September 2015 / Revised: 27 November 2015 / Accepted: 17 February 2016 / Published: 3 March 2016
(This article belongs to the Special Issue Membrane Protein Based Biosensors)
His-tag technology was applied for biosensing purposes involving multi-redox center proteins (MRPs). An overview is presented on various surfaces ranging from flat to spherical and modified with linker molecules with nitrile-tri-acetic acid (NTA) terminal groups to bind his-tagged proteins in a strict orientation. The bound proteins are submitted to in situ dialysis in the presence of lipid micelles to form a so-called protein-tethered bilayer lipid membrane (ptBLM). MRPs, such as the cytochrome c oxidase (CcO) from R. sphaeroides and P. denitrificans, as well as photosynthetic reactions centers (RCs) from R. sphaeroides, were thus investigated. Electrochemical and surface-sensitive optical techniques, such as surface plasmon resonance, surface plasmon-enhanced fluorescence, surface-enhanced infrared absorption spectroscopy (SEIRAS) and surface-enhanced resonance Raman spectroscopy (SERRS), were employed in the case of the ptBLM structure on flat surfaces. Spherical particles ranging from µm size agarose gel beads to nm size nanoparticles modified in a similar fashion were called proteo-lipobeads (PLBs). The particles were investigated by laser-scanning confocal fluorescence microscopy (LSM) and UV/Vis spectroscopy. Electron and proton transfer through the proteins were demonstrated to take place, which was strongly affected by the membrane potential. MRPs can thus be used for biosensing purposes under quasi-physiological conditions. View Full-Text
Keywords: multi-redox center proteins; protein-tethered bilayer lipid membrane; cytochrome c oxidase; photosynthetic reaction centers; surface-enhanced infrared absorption spectroscopy; surface-enhanced resonance Raman spectroscopy; laser-scanning confocal microscopy; UV/Vis spectroscopy; his-tag technology; proteo-lipobeads multi-redox center proteins; protein-tethered bilayer lipid membrane; cytochrome c oxidase; photosynthetic reaction centers; surface-enhanced infrared absorption spectroscopy; surface-enhanced resonance Raman spectroscopy; laser-scanning confocal microscopy; UV/Vis spectroscopy; his-tag technology; proteo-lipobeads
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Naumann, R.L.C.; Geiss, A.F.; Steininger, C.; Knoll, W. Biomimetic Membranes for Multi-Redox Center Proteins. Int. J. Mol. Sci. 2016, 17, 330.

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