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Orientation-Controlled Electrocatalytic Efficiency of an Adsorbed Oxygen-Tolerant Hydrogenase
Citation key Heidary2015
Author Heidary, N. and Utesch, T. and Zerball, M. and Horch, M. and Millo, D. and Fritsch, J. and Lenz, O. and von Klitzing, R. and Hildebrandt, P. and Fischer, A. and Mroginski, M. A. and Zebger, I.
Pages e0143101
Year 2015
DOI 10.1371/journal.pone.0143101
Journal Plos One
Volume 10
Number 11
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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