Edwards, Marcus J and Gates, Andrew J and Butt, Julea N and Richardson, David J and Clarke, Thomas A (2017) 'Comparative structure-potentio-spectroscopy of the Shewanella outer membrane multiheme cytochromes.' Current Opinion in Electrochemistry, 4 (1). pp. 199-205. ISSN 2451-9103

Preview

Text 1-s2.0-S2451910317301229-main.pdf - Published Version Available under License Creative Commons Attribution. Download (1MB) | Preview

Abstract

Many species of bacteria can generate energy in the anoxic subsurface by directly coupling intracellular oxidative reactions to the reduction of extracellular metal oxides. Coupling these processes requires electron transfer networks that extend from the inside of the cell, across the outer membrane to the extracellular terminal electron acceptors. The best described of these networks is from Shewanella oneidensis MR-1, where four structures of outer membrane multiheme cytochromes (OMMCs) have been determined. These OMMCs contain 10–11 bis-histidine-ligated c-type hemes and are directly involved in the reduction of iron and manganese oxides at the cell surface. The heme ligands for some of these structures have been characterised using electron paramagnetic resonance (EPR), the redox properties have been mapped by protein film electrochemistry (PFE) and more recently molecular dynamic simulations have been used to obtain microscopic redox potentials for individual heme groups. This review maps these different experimental techniques onto the structures, providing insight into the intramolecular electron transfer pathways of OMMCs, revealing future directions for study.

Item Type:	Article
Divisions:	Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of
SWORD Depositor:	Elements
Depositing User:	Elements
Date Deposited:	09 Dec 2020 11:33
Last Modified:	18 Aug 2022 13:06
URI:	http://repository.essex.ac.uk/id/eprint/29308

Actions (login required)

View Item