McMillan, DGG, Jeuken, LJC, Marritt, SJ et al. (3 more authors) (2013) The impact of enzyme orientation and electrode topology on the catalytic activity of adsorbed redox enzymes. Electrochimica Acta, 110. 79 - 85. ISSN 0013-4686
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 SnO 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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2013, Elsevier. NOTICE: this is the author’s version of a work that was accepted for publication in Electrochimica Acta. Changes resulting from the publishing process, such as peer review, editing, corrections, structural formatting, and other quality control mechanisms may not be reflected in this document. Changes may have been made to this work since it was submitted for publication. A definitive version was subsequently published in Electrochimica Acta, 110, 2013. http://dx.doi.org/10.1016/j.electacta.2013.01.153 |
Keywords: | Self-assembled monolayer (SAM); Protein-film electrochemistry (PFE); Cytochrome; Quinone; Lipid vesicle |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Medicine and Health (Leeds) > School of Medicine (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 18 Mar 2014 10:59 |
Last Modified: | 29 Mar 2018 12:46 |
Published Version: | http://dx.doi.org/10.1016/j.electacta.2013.01.153 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/j.electacta.2013.01.153 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:78095 |