XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode
High potential purified Trametes trogii laccase has been deposited in mono- and multilayer thin films on gold surfaces by layer-by-layer electrostatic adsorption self-assembly. The osmium bipyridil redox relay sites on polycation poly(allylamine) backbone efficiently work as a molecular "wire&q...
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paper:paper_00032700_v86_n24_p12180_Scodeller2023-06-08T14:24:14Z XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode Scodeller, Pablo David Williams, Federico Jose Calvo, Ernesto Julio Adsorption Biofuels Biological fuel cells Electrodes Enzyme electrodes Enzymes Film preparation Gold deposits Molecular oxygen Multilayer films Multilayers Osmium Quartz Self assembly Chemical equations Chemical identity Chemical information Electrical charges Electrostatic adsorption Mono- and multilayer Oxidation-reduction cycle Surface concentration X ray photoelectron spectroscopy enzymes, immobilized Laccase chemistry electrodes enzymology methods Oxidation-Reduction Photoelectron Spectroscopy Trametes Electrodes Enzymes, Immobilized Laccase Oxidation-Reduction Photoelectron Spectroscopy Trametes High potential purified Trametes trogii laccase has been deposited in mono- and multilayer thin films on gold surfaces by layer-by-layer electrostatic adsorption self-assembly. The osmium bipyridil redox relay sites on polycation poly(allylamine) backbone efficiently work as a molecular "wire" in oxygen cathodes for biofuel cells. X-ray photoelectron spectroscopy of Cu 2p3/2 and Os 4f signals provided chemical information on the enzyme and redox mediator surface concentrations after different adsorption steps. The electrical charge involved in oxidation-reduction cycles of the osmium sites, the ellipsometric enzyme film thickness, and the mass uptake from quartz crystal microbalance experiments, correlate with the XPS surface concentration, which provides unique evidence on the chemical identity of the composition in the topmost layers. XPS is shown to be an important analytical tool to investigate stratified copper and osmium distribution in LbL thin films relevant to biosensors and biofuel cells. (Chemical Equation Presented). © 2014 American Chemical Society. Fil:Scodeller, P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Williams, F.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Calvo, E.J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2014 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032700_v86_n24_p12180_Scodeller http://hdl.handle.net/20.500.12110/paper_00032700_v86_n24_p12180_Scodeller |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Adsorption Biofuels Biological fuel cells Electrodes Enzyme electrodes Enzymes Film preparation Gold deposits Molecular oxygen Multilayer films Multilayers Osmium Quartz Self assembly Chemical equations Chemical identity Chemical information Electrical charges Electrostatic adsorption Mono- and multilayer Oxidation-reduction cycle Surface concentration X ray photoelectron spectroscopy enzymes, immobilized Laccase chemistry electrodes enzymology methods Oxidation-Reduction Photoelectron Spectroscopy Trametes Electrodes Enzymes, Immobilized Laccase Oxidation-Reduction Photoelectron Spectroscopy Trametes |
| spellingShingle |
Adsorption Biofuels Biological fuel cells Electrodes Enzyme electrodes Enzymes Film preparation Gold deposits Molecular oxygen Multilayer films Multilayers Osmium Quartz Self assembly Chemical equations Chemical identity Chemical information Electrical charges Electrostatic adsorption Mono- and multilayer Oxidation-reduction cycle Surface concentration X ray photoelectron spectroscopy enzymes, immobilized Laccase chemistry electrodes enzymology methods Oxidation-Reduction Photoelectron Spectroscopy Trametes Electrodes Enzymes, Immobilized Laccase Oxidation-Reduction Photoelectron Spectroscopy Trametes Scodeller, Pablo David Williams, Federico Jose Calvo, Ernesto Julio XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| topic_facet |
Adsorption Biofuels Biological fuel cells Electrodes Enzyme electrodes Enzymes Film preparation Gold deposits Molecular oxygen Multilayer films Multilayers Osmium Quartz Self assembly Chemical equations Chemical identity Chemical information Electrical charges Electrostatic adsorption Mono- and multilayer Oxidation-reduction cycle Surface concentration X ray photoelectron spectroscopy enzymes, immobilized Laccase chemistry electrodes enzymology methods Oxidation-Reduction Photoelectron Spectroscopy Trametes Electrodes Enzymes, Immobilized Laccase Oxidation-Reduction Photoelectron Spectroscopy Trametes |
| description |
High potential purified Trametes trogii laccase has been deposited in mono- and multilayer thin films on gold surfaces by layer-by-layer electrostatic adsorption self-assembly. The osmium bipyridil redox relay sites on polycation poly(allylamine) backbone efficiently work as a molecular "wire" in oxygen cathodes for biofuel cells. X-ray photoelectron spectroscopy of Cu 2p3/2 and Os 4f signals provided chemical information on the enzyme and redox mediator surface concentrations after different adsorption steps. The electrical charge involved in oxidation-reduction cycles of the osmium sites, the ellipsometric enzyme film thickness, and the mass uptake from quartz crystal microbalance experiments, correlate with the XPS surface concentration, which provides unique evidence on the chemical identity of the composition in the topmost layers. XPS is shown to be an important analytical tool to investigate stratified copper and osmium distribution in LbL thin films relevant to biosensors and biofuel cells. (Chemical Equation Presented). © 2014 American Chemical Society. |
| author |
Scodeller, Pablo David Williams, Federico Jose Calvo, Ernesto Julio |
| author_facet |
Scodeller, Pablo David Williams, Federico Jose Calvo, Ernesto Julio |
| author_sort |
Scodeller, Pablo David |
| title |
XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| title_short |
XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| title_full |
XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| title_fullStr |
XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| title_full_unstemmed |
XPS analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| title_sort |
xps analysis of enzyme and mediator at the surface of a layer-by-layer self-assembled wired enzyme electrode |
| publishDate |
2014 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00032700_v86_n24_p12180_Scodeller http://hdl.handle.net/20.500.12110/paper_00032700_v86_n24_p12180_Scodeller |
| work_keys_str_mv |
AT scodellerpablodavid xpsanalysisofenzymeandmediatoratthesurfaceofalayerbylayerselfassembledwiredenzymeelectrode AT williamsfedericojose xpsanalysisofenzymeandmediatoratthesurfaceofalayerbylayerselfassembledwiredenzymeelectrode AT calvoernestojulio xpsanalysisofenzymeandmediatoratthesurfaceofalayerbylayerselfassembledwiredenzymeelectrode |
| _version_ |
1768542341665128448 |