An operationally simple and highly selective method for the decarboxylation of fatty acids under remarkably mild conditions is described herein. The activation of the aliphatic carboxylic acids by esterification with -hydroxyphthalimide (NHPI) enabled efficient deoxygenation to synthesize -alkanes in up to 67% yield, employing inexpensive PMHS as a hydrogen source, NiCl·6HO, bipyridine, and zinc in THF. In contrast to the conventional thermo-catalytic approaches, this protocol does not require high temperature and high pressure of hydrogen gas to deoxygenate biomass-derived carboxylic acids, thus representing an attractive alternative for producing drop-in biofuels.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9521194 | PMC |
http://dx.doi.org/10.1039/d2ra04057c | DOI Listing |
Nanomaterials (Basel)
December 2024
Center for Genomics and Precision Medicine, Institute of Bioscience and Technology, Texas A&M Health Science Center, Houston, TX 77030, USA.
Our group has synthesized a pleiotropic synthetic nanozyme redox mediator we term a "pleozyme" that displays multiple enzymatic characteristics, including acting as a superoxide dismutase mimetic, oxidizing NADH to NAD, and oxidizing HS to polysulfides and thiosulfate. Benefits have been seen in acute and chronic neurological disease models. The molecule is sourced from coconut-derived activated charcoal that has undergone harsh oxidization with fuming nitric acid, which alters the structure and chemical characteristics, yielding 3-8 nm discs with broad redox potential.
View Article and Find Full Text PDFBiochim Biophys Acta Mol Cell Biol Lipids
December 2024
Department of Chemistry and Biochemistry, Villanova University, Villanova, PA 19085, USA. Electronic address:
An open reading frame from the actinobacterium Mycolicibacterium smegmatis annotated as a Prostaglandin H Synthase (PGHS) was expressed with an N-terminal (his) tag and purified to homogeneity. The enzyme has a monomeric molecular weight of 68.3 kD and exists as a dimer in the presence of nonionic detergent.
View Article and Find Full Text PDFInt J Mol Sci
October 2024
Department of Biochemistry, Faculty of Medicine, Medical University of Gdansk, 80-211 Gdansk, Poland.
Lipid metabolism in various adipose tissue depots can differ vastly. This also applies to lipogenesis, the process of synthesizing fatty acids from acetyl-CoA. This study compared the expression of some lipogenic enzymes: fatty acid synthase (FASN), ATP-citrate lyase (ACLY), and malic enzyme 1 (ME1) in different regions of the posterior subcutaneous adipose tissue in rats.
View Article and Find Full Text PDFbioRxiv
October 2024
Department of Cellular and Developmental Biology, Department of Surgery, Faculty of Medicine, University of British Columbia, Vancouver, BC, Canada.
Pyruvate dehydrogenase kinase (PDK) 1 is one of four isozymes that inhibit the oxidative decarboxylation of pyruvate to acetyl-CoA via pyruvate dehydrogenase. PDK activity is elevated in fasting or starvation conditions to conserve carbohydrate reserves. PDK has also been shown to increase mitochondrial fatty acid utilization.
View Article and Find Full Text PDFChembiochem
December 2024
Institute of Chemistry, University of Graz, Heinrichstraße 28, 8010, Graz, Austria.
Light-dependent fatty acid photodecarboxylases (FAPs) hold significant potential for biotechnology, due to their capability to produce alka(e)nes directly from the corresponding (un)saturated natural fatty acids requiring light as the only reagent. This study expands the family of FAPs through cavity-based enzyme discovery methods. Thirty enzyme candidates with potential photodecarboxylation activity were identified by matching the cavities of four related template structures against the Protein Data Bank's flavoproteins, a library of proteins identified via the Foldseek Search Server, and homology models of sequences resulting from BLAST.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!