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MftG is crucial for ethanol metabolism of mycobacteria by linking mycofactocin oxidation to respiration.
Elife
January 2025
Leibniz Institute for Natural Product Research and Infection Biology - Hans Knöll Institute, Junior Research Group Synthetic Microbiology, Jena, Germany.
Mycofactocin is a redox cofactor essential for the alcohol metabolism of mycobacteria. While the biosynthesis of mycofactocin is well established, the gene , which encodes an oxidoreductase of the glucose-methanol-choline superfamily, remained functionally uncharacterized. Here, we show that MftG enzymes are almost exclusively found in genomes containing mycofactocin biosynthetic genes and are present in 75% of organisms harboring these genes.
View Article and Find Full Text PDFThe effect of histidine, histamine, and imidazole on electrochemical properties of Cu(II) complexes of Aβ peptides containing His-2 and His-3 motifs.
Dalton Trans
September 2024
Chair of Medical Biotechnology, Faculty of Chemistry, Warsaw University of Technology, Noakowskiego 3, 00-664 Warsaw, Poland.
The N-truncation of amyloid beta (Aβ) peptides could lead to peptide sequences with the histidine residue at the second and third positions, creating His-2 and His-3 motifs, known as high-affinity Cu(II) binding sites. In such complexes, the Cu(II) ion is arrested in a rigid structure of a square-planar arrangement of nitrogen donors, which highly limits its susceptibility to Cu(II) reduction. Cu(II) reduction fuels the Cu(II)/Cu(I) redox cycle, which is engaged in the production of reactive oxygen species (ROS).
View Article and Find Full Text PDFRedox-Triggered Reversible Switching between Dynamic and Quasi-static α-Helical Peptides.
Chemistry
October 2024
Nano Life Science Institute (WPI-NanoLSI), Kakuma-machi, Kanazawa University, 920-1192, Kanazawa, Japan.
We report the reversible transformation between a singly stapled dynamic α-helical peptide and a doubly stapled quasi-static one through redox-triggered dithiol/disulfide conversions of a stapling moiety. This process allows the rate of interconversion between the right-handed (P) and left-handed (M) α-helices to be altered by a factor of approximately 10 before and after the transformation. An as-obtained doubly stapled α-helical peptide, which is composed of an achiral peptide having an l-valine carboxylic acid residue at the C-terminus, a disulfide-based reversible staple, and a biphenyl-based fixed staple, adopts an (M)-rich form as a kinetically trapped state.
View Article and Find Full Text PDFPlant Life with and without Oxygen: A Metabolomics Approach.
Int J Mol Sci
November 2023
Department of Plant Physiology and Biochemistry, Faculty of Biology, St. Petersburg State University, 199034 St. Petersburg, Russia.
Oxygen deficiency is an environmental challenge which affects plant growth, the development and distribution in land and aquatic ecosystems, as well as crop yield losses worldwide. The capacity to exist in the conditions of deficiency or the complete lack of oxygen depends on a number of anatomic, developmental and molecular adaptations. The lack of molecular oxygen leads to an inhibition of aerobic respiration, which causes energy starvation and the acceleration of glycolysis passing into fermentations.
View Article and Find Full Text PDFThe role of glutathione in periplasmic redox homeostasis and oxidative protein folding in Escherichia coli.
Redox Biol
August 2023
Ruhr University Bochum, Institute of Biochemistry and Pathobiochemistry, Microbial Biochemistry, Bochum, Germany. Electronic address:
The thiol redox balance in the periplasm of E. coli depends on the DsbA/B pair for oxidative power and the DsbC/D system as its complement for isomerization of non-native disulfides. While the standard redox potentials of those systems are known, the in vivo "steady state" redox potential imposed onto protein thiol disulfide pairs in the periplasm remains unknown.
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