Jeuken, LJC, Connell, SD, Nurnabi, M et al. (4 more authors) (2005) Direct electrochemical interaction between a modified gold electrode and a bacterial membrane extract. Langmuir, 21 (4). 1481 - 1488. ISSN 0743-7463
Abstract
A novel electrochemical approach is described for redox-active membrane proteins. A total membrane extract (in the form of vesicles) of Bacillus subtilis is tethered onto gold surfaces modified with cholesterol based thiols. The membrane vesicles remain intact on the surface and do not rupture or fuse to form a planar bilayer. Oxidation/reduction signals are obtained of the natural co-enzyme, menaquinone-7, located in the membrane. The membrane protein, succinate menaquinone oxidoreductase (SQR), remains in the vesicles and is able to reduce fumarate using menaquinone as mediator. The catalysis of the reverse reaction (oxidation of succinate), which is the natural catalytic function of SQR, is almost absent with menaquinone. However, adding the co-enzyme ubiquinone, which has a reduction potential that is about 0.2 V higher, restores the succinate oxidation activity.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | (c) 2005, American Chemical Society. This is an author produced version of a paper published in Langmuir. Uploaded with permission from the publisher. |
Keywords: | Self-Assembled Monolayers; Lipid-Bilayer-Membranes; Cytochrome-C-Oxidase; Bacillus-Subtilis; Direct Bioelectrocatalysis; Succinate-Dehydrogenase; Alcohol-Dehydrogenase; Escherichia-Coli; Menaquinone; Oxidoreductase |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Chemistry (Leeds) The University of Leeds > Faculty of Engineering & Physical Sciences (Leeds) > School of Physics and Astronomy (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 21 Nov 2013 17:47 |
Last Modified: | 15 Sep 2014 02:42 |
Published Version: | http://dx.doi.org/10.1021/la047732f |
Status: | Published |
Publisher: | American Chemical Society |
Identification Number: | 10.1021/la047732f |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:77056 |