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Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase

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
Article, Secondary publication, Publisher's Version

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.

Item Type: Article
Erschienen: 2021
Creators: 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
Type of entry: Secondary publication
Title: Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase
Language: English
Date: 2021
Year of primary publication: 2015
Publisher: PLOS
Journal or Publication Title: PLOS ONE
Volume of the journal: 10
Issue Number: 11
Collation: 9 Seiten
DOI: 10.26083/tuprints-00019058
URL / URN: https://tuprints.ulb.tu-darmstadt.de/19058
Corresponding Links:
Origin: Secondary publication service
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: Publisher's Version
URN: urn:nbn:de:tuda-tuprints-190580
Classification DDC: 500 Science and mathematics > 530 Physics
Divisions: 05 Department of Physics
05 Department of Physics > Institute for Condensed Matter Physics
Date Deposited: 11 Aug 2021 13:05
Last Modified: 16 Aug 2021 07:24
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