The impact of enzyme orientation and electrode topology on the catalytic activity of adsorbed redox enzymes

Mcmillan, Duncan G.G., Marritt, Sophie J., Kemp, Gemma L., Gordon-Brown, Piers, Butt, Julea N. and Jeuken, Lars J.C. (2013) The impact of enzyme orientation and electrode topology on the catalytic activity of adsorbed redox enzymes. Electrochimica Acta, 110. pp. 79-85. ISSN 0013-4686

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Abstract

It is well established that the structural details of electrodes and their interaction with adsorbed enzyme influences the interfacial electron transfer rate. However, for nanostructured electrodes, it is likely that the structure also impacts on substrate flux near the adsorbed enzymes and thus catalytic activity. Furthermore, for enzymes converting macro-molecular substrates it is possible that the enzyme orientation determines the nature of interactions between the adsorbed enzyme and substrate and therefore catalytic rates. In essence the electrode may impede substrate access to the active site of the enzyme. We have tested these possibilities through studies of the catalytic performance of two enzymes adsorbed on topologically distinct electrode materials. Escherichia coli NrfA, a nitrite reductase, was adsorbed on mesoporous, nanocrystalline SnO2 electrodes. CymA from Shewanella oneidensis MR-1 reduces menaquinone-7 within 200 nm sized liposomes and this reaction was studied with the enzyme adsorbed on SAM modified ultra-flat gold electrodes.

Item Type: Article
Uncontrolled Keywords: self-assembled monolayer (sam),protein-film electrochemistry (pfe),cytochrome,quinone,lipid vesicle
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Medicine and Health Sciences > Norwich Medical School
Faculty of Science > School of Biological Sciences
Depositing User: Pure Connector
Date Deposited: 11 Nov 2013 16:18
Last Modified: 17 Sep 2020 23:53
URI: https://ueaeprints.uea.ac.uk/id/eprint/44389
DOI: 10.1016/j.electacta.2013.01.153

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