Certain bacterial species have a natural ability to exchange electrons with extracellular redox partners. This behavior allows coupling of catalytic transformations inside bacteria to complementary redox transformations of catalysts and electrodes outside the cell. Electricity generation can be coupled to waste-water remediation. Industrially relevant oxidation reactions can proceed exclusively when electrons are released to anodes. Reduced products such as fuels can be generated when electrons are provided from (photo)cathodes. Rational development of these opportunities and inspiration for novel technologies is underpinned by resolution at the molecular level of pathways supporting electron exchange across bacterial cell envelopes. This chapter describes methods for purification, engineering, and in vitro characterization of proteins providing the primary route for electron transport across the outer membrane lipid bilayer of Shewanella oneidensis MR-1, a well-described electrogenic bacterium and chassis organism for related biotechnologies.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/bs.mie.2018.10.011 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Unraveling the Membrane Topology of TMEM151A: A Step Towards Understanding its Cellular Role.
J Mol Biol
December 2024
University of Genova, Department of Experimental Medicine, Genova, Italy; IRCCS Ospedale Policlinico San Martino, Genova, Italy. Electronic address:
Transmembrane protein 151A (TMEM151A) has been identified as a causative gene for paroxysmal kinesigenic dyskinesia, though its molecular function remains almost completely unknown. Understanding the membrane topology of transmembrane proteins is crucial for elucidating their functions and possible interacting partners. In this study, we utilized molecular dynamics simulations, immunocytochemistry, and electron microscopy to define the topology of TMEM151A.
View Article and Find Full Text PDFComputational Insights into the Non-Heme Diiron Alkane Monooxygenase Enzyme AlkB: Electronic Structures, Dioxygen Activation, and Hydroxylation Mechanism of Liquid Alkanes.
Inorg Chem
September 2024
School of Chemistry and Chemical Engineering, Shandong University, Jinan, Shandong 250100, China.
Alkane monooxygenase (AlkB) is a membrane-spanning metalloenzyme that catalyzes the terminal hydroxylation of straight-chain alkanes involved in the microbially mediated degradation of liquid alkanes. According to the cryoEM structures, AlkB features a unique multihistidine ligand coordination environment with a long Fe-Fe distance in its active center. Up to now, how AlkB employs the diiron center to activate dioxygen and which species is responsible for triggering the hydroxylation are still elusive.
View Article and Find Full Text PDFMolecular architecture of coronavirus double-membrane vesicle pore complex.
Nature
September 2024
School of Biomedical Sciences, Li Ka Shing Faculty of Medicine, The University of Hong Kong, Hong Kong SAR, China.
Article Synopsis
- * The study reveals the structure of the nsp3-nsp4 pore complex, consisting of 12 nsp3 and 12 nsp4 proteins organized in a way similar to a nuclear pore complex, facilitating RNA transport.
- * This research sheds light on how DMVs and RNA transport are formed, laying the groundwork for developing new antiviral treatments against coronavirus infections.
Dissecting structure and function of the monovalent cation/H antiporters Mdm38 and Ylh47 in .
J Bacteriol
August 2024
Graduate School of Engineering, Tohoku University, Aobayama, Sendai, Japan.
Unlabelled: Mdm38 and Ylh47 are homologs of the Ca/H antiporter Letm1, a candidate gene for seizures associated with Wolf-Hirschhorn syndrome in humans. Mdm38 is important for K/H exchange across the inner mitochondrial membrane and contributes to membrane potential formation and mitochondrial protein translation. Ylh47 also localizes to the inner mitochondrial membrane.
View Article and Find Full Text PDFBiosynthesis of GMGT lipids by a radical SAM enzyme associated with anaerobic archaea and oxygen-deficient environments.
Nat Commun
June 2024
Department of Ocean Science and Engineering, Southern University of Science and Technology, Shenzhen, China.
Archaea possess characteristic membrane-spanning lipids that are thought to contribute to the adaptation to extreme environments. However, the biosynthesis of these lipids is poorly understood. Here, we identify a radical S-adenosyl-L-methionine (SAM) enzyme that synthesizes glycerol monoalkyl glycerol tetraethers (GMGTs).
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!