Iron-Mediated Segment Coupling of Alkenols with Acceptors via C-C Radical Translocation and Remote Oxidative 1,5/6-Hydrogen Atom Transfer.

Iron-mediated segment coupling followed by oxidative 1,5/6-hydrogen atom transfer (HAT) for synthesis of ε-oxo alkene derivatives is developed. This transformation involved translocation of the radical from H-to-C-to-C-to-C followed by the oxidation under MHAT conditions providing rapid access to 1,6/1,7-keto functionalized esters/ketone/sulfones/phosphonates/arenes. The different outcomes of coupling with acceptors could be explained by bond dissociation energies (BDEs), and mechanistic insights were gained through control experiments, including deuterium labeling studies.

Iodine(III)-Mediated Keto-oximation of -Alkynyl Hydroxylamines: A Route to 3-Acyl Isoxazolines and 1,2-Oxazines.

An intramolecular iodine(III)-mediated keto-oximation of -alkynyl hydroxylamines offers rapid and straightforward access to 3-acyl Δ-isoxazolines and 1,2-oxazines. This approach features mild, metal-free, and aerobic reaction conditions with good functional group tolerance. Moreover, the synthetic utility of this method is demonstrated by the synthesis of unique structural motifs such as isoxazolidine, 3-vinyl isoxazoline, and 2,5-diphenylpyrazine derivatives by the conversion of 3-acyl Δ-isoxazolines, thereby showcasing its efficiency and applicability in synthetic chemistry.

Unlocking a reductive hydroalkoxylation cascade for the stereoselective synthesis of cyclic ethers: total synthesis of (±)-isolaurepan and (±)--lauthisan.

A Lewis acid-mediated, 5/6/7/8- reductive hydroalkoxylation cascade on enynols gives expeditious, diastereoselective access to small and medium ring cyclic ethers with a long aliphatic side chain. The brevity of the approach allowed a 4-step, stereoselective total synthesis of (±)-isolaurepan and (±)--lauthisan.

Proximity labeling defines the phagosome lumen proteome of murine and primary human macrophages.

Proteomic analyses of the phagosome has significantly improved our understanding of the proteins which contribute to critical phagosome functions such as apoptotic cell clearance and microbial killing. However, previous methods of isolating phagosomes for proteomic analysis have relied on cell fractionation with some intrinsic limitations. Here, we present an alternative and modular proximity-labeling based strategy for mass spectrometry proteomic analysis of the phagosome lumen, termed PhagoID.