Development of a proteoliposome model to probe transmembrane electron-transfer reactions

White, Gaye F., Shi, Zhi, Shi, Liang, Dohnalkova, Alice C., Fredrickson, James K., Zachara, John M., Butt, Julea N. ORCID: https://orcid.org/0000-0002-9624-5226, Richardson, David J. ORCID: https://orcid.org/0000-0002-6847-1832 and Clarke, Thomas A. ORCID: https://orcid.org/0000-0002-6234-1914 (2012) Development of a proteoliposome model to probe transmembrane electron-transfer reactions. Biochemical Society Transactions, 40 (6). pp. 1257-1260. ISSN 0300-5127

[thumbnail of White_et_al_Biochem_Soc_Trans_2012_Development_of_a_model_for.pdf]
Preview
PDF (White_et_al_Biochem_Soc_Trans_2012_Development_of_a_model_for.pdf)
Download (252kB) | Preview

Abstract

The mineral-respiring bacterium Shewanella oneidensis uses a protein complex, MtrCAB, composed of two decahaem cytochromes brought together inside a transmembrane porin to transport electrons across the outer membrane to a variety of mineral-based electron acceptors. A proteoliposome system has been developed that contains Methyl Viologen as an internalized electron carrier and valinomycin as a membrane-associated cation exchanger. These proteoliposomes can be used as a model system to investigate MtrCAB function.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
Faculty of Science > School of Chemistry
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017)
Faculty of Science > Research Groups > Organisms and the Environment
Faculty of Science > Research Groups > Chemistry of Light and Energy
Faculty of Science > Research Groups > Chemistry of Life Processes
Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry
Faculty of Science > Research Groups > Energy Materials Laboratory
Depositing User: Sophie Buckingham
Date Deposited: 25 Mar 2013 16:50
Last Modified: 10 Mar 2024 00:42
URI: https://ueaeprints.uea.ac.uk/id/eprint/41981
DOI: 10.1042/BST20120116

Actions (login required)

View Item View Item