Bespoke Biomolecular Wires for Transmembrane Electron Transfer: Spontaneous Assembly of a Functionalized Multiheme Electron Conduit.

Autor:	Piper SEH; School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich, United Kingdom., Edwards MJ; School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich, United Kingdom., van Wonderen JH; School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich, United Kingdom., Casadevall C; Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Martel A; Institut Laue-Langevin, Grenoble, France., Jeuken LJC; School of Biomedical Sciences, University of Leeds, Leeds, United Kingdom., Reisner E; Yusuf Hamied Department of Chemistry, University of Cambridge, Cambridge, United Kingdom., Clarke TA; School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich, United Kingdom., Butt JN; School of Chemistry and School of Biological Sciences, University of East Anglia, Norwich, United Kingdom.
Jazyk:	angličtina
Zdroj:	Frontiers in microbiology [Front Microbiol] 2021 Aug 16; Vol. 12, pp. 714508. Date of Electronic Publication: 2021 Aug 16 (Print Publication: 2021).
DOI:	10.3389/fmicb.2021.714508
Abstrakt:	Shewanella oneidensis exchanges electrons between cellular metabolism and external redox partners in a process that attracts much attention for production of green electricity (microbial fuel cells) and chemicals (microbial electrosynthesis). A critical component of this pathway is the outer membrane spanning MTR complex, a biomolecular wire formed of the MtrA, MtrB, and MtrC proteins. MtrA and MtrC are decaheme cytochromes that form a chain of close-packed hemes to define an electron transfer pathway of 185 Å. MtrA is wrapped inside MtrB for solubility across the outer membrane lipid bilayer; MtrC sits outside the cell for electron exchange with external redox partners. Here, we demonstrate tight and spontaneous in vitro association of MtrAB with separately purified MtrC. The resulting complex is comparable with the MTR complex naturally assembled by Shewanella in terms of both its structure and rates of electron transfer across a lipid bilayer. Our findings reveal the potential for building bespoke electron conduits where MtrAB combines with chemically modified MtrC, in this case, labeled with a Ru-dye that enables light-triggered electron injection into the MtrC heme chain. Competing Interests: The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. (Copyright © 2021 Piper, Edwards, van Wonderen, Casadevall, Martel, Jeuken, Reisner, Clarke and Butt.)
Databáze:	MEDLINE
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