Part:BBa_K4849014
MtrB - periplasmic decaheme cytochrome protein
An outer membrane β-barrel protein facilitating transport of electrons from the periplasm to outside of the cell. MtrB protein is a transmembrane porin sitting between MtrA (cell side) and MtrC (outer side). (as seen in the illustration)
Metal-reducing microorganisms such as Shewanella oneidensis MR-1 and Geobacter metallireducens have evolved an innate EET pathway that makes them ideal for bioelectricity applications. The most characterised EET pathway in S. oneidensis MR-1 includes MtrCAB complex. Based on the current understanding, the electrons extracted from the oxidation of a substrate are ultimately transferred to the periplasmic decaheme cytochrome MtrA during anaerobic respiration. Subsequent electron transfer to the outer membrane β-barrel protein MtrB places MtrA in direct contact with MtrC. MtrC is re-oxidised by reducing terminal electron acceptors, such as electrodes, via direct or mediated electron transfer.
Image made in Biorender.com
White, Gaye, et al. "Rapid Electron Exchange between Surface-Exposed Bacterial Cytochromes and Fe(III) Minerals." Proceedings of the National Academy of Sciences, vol. 110, no. 16, 2013, pp. 6346-6351
References:
1. Ross, Daniel E., et al. "Characterization of protein-protein interactions involved in iron reduction by Shewanella oneidensis MR-1." Applied and environmental microbiology 73.18 (2007): 5797-5808.
2. Breuer, Marian, et al. "Multi-haem cytochromes in Shewanella oneidensis MR-1: structures, functions and opportunities." Journal of The Royal Society Interface 12.102 (2015): 20141117.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
| None |