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Chair of Biochemistry of Microorganisms at University of Bayreuth (Kulmbach). Topics: Microbes, bioactive natural products and synthetic biology
What the f* is mycofactocin?
If you’ve ever wondered about the unusual cofactor – wonder no more. We’ve written up a review article for NPR covering its discovery, biosynthesis, and biological roles. Huge thanks to all co-authors who made this happen!
https://pubs.rsc.org/en/content/articlelanding/2025/np/d5np00012b
Great to see our article about the role of MftG in mycobacterial respiration highlighted in eLife: https://doi.org/10.7554/eLife.106286
Cellular Energy Production: Mycofactocin and the mycobacterial electron transport chain

In the bacterium M. smegmatis, an enzyme called MftG allows the cofactor mycofactocin to transfer electrons released during ethanol metabolism to the electron transport chain.

eLife
Curious how tuberculosis-related mycobacteria process alcohol? We have identified a novel enzyme that couples ethanol metabolism to respiration in these organisms. Many thanks to all authors and our collaborators from the Papenfort and Vilotijevic labs!
https://doi.org/10.7554/eLife.97559.4
MftG is crucial for ethanol metabolism of mycobacteria by linking mycofactocin oxidation to respiration

The mftG gene, present in the majority of mycofactocin gene clusters, encodes an oxidoreductase that facilitates ethanol utilization by reoxidation of mycofactocins and channeling electrons towards the respiratory chain.

eLife

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Great paper by the group of Lars Jeuken in J. Biol. Chem. with first author Tijn van der Velden. Cytochrome bd of M. tuberculosis is RedOx-regulated through a disulfide with potential important implications for survival in the phagosome. Exciting insights into the biochemical activity, the substrate specificity and the activation of cytochrome bd as well as an insightful cryoEM structure to better understand the role of the critical, RedOx-regulated disulfide.
https://www.jbc.org/article/S0021-9258(24)02596-1/fulltext