Heidary, Nina ; Utesch, Tillmann ; Zerball, Maximilian ; Horch, Marius ; Millo, Diego ; Fritsch, Johannes ; Lenz, Oliver ; Klitzing, Regine von ; Hildebrandt, Peter ; Fischer, Anna ; Mroginski, Maria Andrea ; Zebger, Ingo (2021)
Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase.
In: PLOS ONE, 2015, 10 (11)
doi: 10.26083/tuprints-00019058
Artikel, Zweitveröffentlichung, Verlagsversion
Kurzbeschreibung (Abstract)
Protein immobilization on electrodes is a key concept in exploiting enzymatic processes for bioelectronic devices. For optimum performance, an in-depth understanding of the enzyme-surface interactions is required. Here, we introduce an integral approach of experimental and theoretical methods that provides detailed insights into the adsorption of an oxygen-tolerant [NiFe] hydrogenase on a biocompatible gold electrode. Using atomic force microscopy, ellipsometry, surface-enhanced IR spectroscopy, and protein film voltammetry, we explore enzyme coverage, integrity, and activity, thereby probing both structure and catalytic H₂ conversion of the enzyme. Electrocatalytic efficiencies can be correlated with the mode of protein adsorption on the electrode as estimated theoretically by molecular dynamics simulations. Our results reveal that pre-activation at low potentials results in increased current densities, which can be rationalized in terms of a potential-induced re-orientation of the immobilized enzyme.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2021 |
| Autor(en): | Heidary, Nina ; Utesch, Tillmann ; Zerball, Maximilian ; Horch, Marius ; Millo, Diego ; Fritsch, Johannes ; Lenz, Oliver ; Klitzing, Regine von ; Hildebrandt, Peter ; Fischer, Anna ; Mroginski, Maria Andrea ; Zebger, Ingo |
| Art des Eintrags: | Zweitveröffentlichung |
| Titel: | Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase |
| Sprache: | Englisch |
| Publikationsjahr: | 2021 |
| Publikationsdatum der Erstveröffentlichung: | 2015 |
| Verlag: | PLOS |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | PLOS ONE |
| Jahrgang/Volume einer Zeitschrift: | 10 |
| (Heft-)Nummer: | 11 |
| Kollation: | 9 Seiten |
| DOI: | 10.26083/tuprints-00019058 |
| URL / URN: | https://tuprints.ulb.tu-darmstadt.de/19058 |
| Zugehörige Links: | |
| Herkunft: | Zweitveröffentlichungsservice |
| Kurzbeschreibung (Abstract): | Protein immobilization on electrodes is a key concept in exploiting enzymatic processes for bioelectronic devices. For optimum performance, an in-depth understanding of the enzyme-surface interactions is required. Here, we introduce an integral approach of experimental and theoretical methods that provides detailed insights into the adsorption of an oxygen-tolerant [NiFe] hydrogenase on a biocompatible gold electrode. Using atomic force microscopy, ellipsometry, surface-enhanced IR spectroscopy, and protein film voltammetry, we explore enzyme coverage, integrity, and activity, thereby probing both structure and catalytic H₂ conversion of the enzyme. Electrocatalytic efficiencies can be correlated with the mode of protein adsorption on the electrode as estimated theoretically by molecular dynamics simulations. Our results reveal that pre-activation at low potentials results in increased current densities, which can be rationalized in terms of a potential-induced re-orientation of the immobilized enzyme. |
| Status: | Verlagsversion |
| URN: | urn:nbn:de:tuda-tuprints-190580 |
| Sachgruppe der Dewey Dezimalklassifikatin (DDC): | 500 Naturwissenschaften und Mathematik > 530 Physik |
| Fachbereich(e)/-gebiet(e): | 05 Fachbereich Physik 05 Fachbereich Physik > Institut für Physik Kondensierter Materie (IPKM) |
| Hinterlegungsdatum: | 11 Aug 2021 13:05 |
| Letzte Änderung: | 16 Aug 2021 07:24 |
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