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Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase
Citation key ISI:000365154600083
Author Heidary, Nina and Utesch, Tillmann and Zerball, Maximilian and Horch, Marius and Millo, Diego and Fritsch, Johannes and Lenz, Oliver and von Klitzing, Regine and Hildebrandt, Peter and Fischer, Anna and Mroginski, Maria Andrea and Zebger, Ingo
Year 2015
ISSN 1932-6203
DOI 10.1371/journal.pone.0143101
Address 1160 BATTERY STREET, STE 100, SAN FRANCISCO, CA 94111 USA
Journal PLOS ONE
Volume 10
Number 11
Month NOV 18
Publisher PUBLIC LIBRARY SCIENCE
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 H-2 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.
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