Reaction of the tri(μ-sulfido)triiron(iii) tris(β-diketiminate) cyclophane complex, FeSL (1), or of the di(μ-sulfido)diiron(iii) complex FeSHL (5), with the related tri(bromide)triiron(ii) complex FeBrL (2) results in electron and ligand redistribution to yield the mixed-ligand multiiron complexes, including FeBrSL (3) and FeBrSHL (4). The cleavage and redistribution observed in these complexes is reminiscent of necessary Fe-S bond cleavage for substrate activation in nitrogenase enzymes, and provides a new perspective on the lability of Fe-S bonds in FeS clusters.
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http://dx.doi.org/10.1039/d0dt03805a | DOI Listing |
BMC Genomics
December 2024
The Key Lab of Animal Disease and Public Health / Luoyang Key Laboratory of Live Carrier Biomaterial and Animal Disease Prevention and Control, Henan University of Science and Technology, Luoyang, Henan, 471023, China.
The H3 subtype of avian influenza virus (AIV) stands out as one of the most prevalent subtypes, posing a significant threat to public health. In this study, a novel triple-reassortant H3N3 AIV designated A/chicken/China/16/2023 (H3N3), was isolated from a sick chicken in northern China. The complete genome of the isolate was determined using next-generation sequencing, and the AIV-like particles were confirmed via transmission electron microscopy.
View Article and Find Full Text PDFJ Phys Chem B
December 2024
Department of Chemistry and Biochemistry, University of Lethbridge, 4401 University Drive West, Lethbridge, Alberta, Canada T1K 3M4.
Despite the remarkable resistance of the nucleic acid phosphodiester backbone to degradation affording genetic stability, the P-O bond must be broken during DNA repair and RNA metabolism, among many other critical cellular processes. Nucleases are powerful enzymes that can enhance the uncatalyzed rate of phosphodiester bond cleavage by up to ∼10-fold. Despite the most well accepted hydrolysis mechanism involving two metals (M to activate a water nucleophile and M to stabilize the leaving group), experimental evidence suggests that some nucleases can use a single metal to facilitate the chemical step, a controversial concept in the literature.
View Article and Find Full Text PDFJ Am Chem Soc
December 2024
Department of Chemistry, University of California Berkeley, Berkeley, California 94720, United States.
In Nature, the four-electron reduction of O is catalyzed at preorganized multimetallic active sites. These complex active sites often feature low-coordinate, redox-active metal centers precisely positioned to facilitate rapid O activation processes that obviate the generation of toxic, partially reduced oxygen species. Very few biomimetic constructs simultaneously recapitulate the complexity and reactivity of these biological cofactors.
View Article and Find Full Text PDFJ Am Chem Soc
December 2024
Catalan Institute of Nanoscience and Nanotechnology (ICN2), CSIC, and Barcelona Institute of Science and Technology, Campus UAB, Bellaterra, Barcelona 08193, Spain.
Herein, we report how merging and clipping nets in metal-organic frameworks (MOFs) can be controlled in a single-crystal-to-single-crystal fashion using three different approaches─the merged net, clip-off chemistry, and linker reinstallation─to design and synthesize three- and two-merged net MOFs. Initially, we show the formation of three isoreticular three-merged net MOFs by linking a trimeric Sc cluster, Sc(μ-Ο)(-COO), with ditopic zigzag and tritopic linkers. The resulting MOFs exhibit three-merged edge-transitive nets─ + + ─for the first time.
View Article and Find Full Text PDFEnviron Microbiol
December 2024
Institute for Environmental Microbiology and Biotechnology, Aquatic Microbiology, University of Duisburg-Essen, Essen, Germany.
The CoA thioester of 2-(carboxymethyl)cyclohexane-1-carboxylic acid has been identified as a metabolite in anaerobic naphthalene degradation by the sulfate-reducing culture N47. This study identified and characterised two acyl-CoA dehydrogenases (ThnO/ThnT) and an intramolecular CoA-transferase (ThnP) encoded within the substrate-induced thn operon, which contains genes for anaerobic degradation of naphthalene. ThnP is a CoA transferase belonging to the family I (Cat 1 subgroup) that catalyses the intramolecular CoA transfer from the carboxyl group of 2-(carboxymethyl)cyclohexane-1-carboxyl-CoA to its carboxymethyl moiety, forming 2-carboxycyclohexylacetyl-CoA.
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