Water oxidation is the key step in both natural and artificial photosynthesis to capture solar energy for fuel production. The design of highly efficient and stable molecular catalysts for water oxidation based on nonprecious metals is still a great challenge. In this article, the electrocatalytic oxidation of water by Na[(L)Co], where L is a substituted tetraamido macrocyclic ligand, was investigated in aqueous solution (pH 7.0). We found that Na[(L)Co] is a stable and efficient homogeneous catalyst for electrocatalytic water oxidation with 380 mV onset overpotential in 0.1 M phosphate buffer (pH 7.0). Both ligand- and metal-centered redox features are involved in the catalytic cycle. In this cycle, Na[(L)Co] was first oxidized to [(L)CoOH] via a ligand-centered proton-coupled electron transfer process in the presence of water. After further losing an electron and a proton, the resting state, [(L)CoOH], was converted to [(L)Co═O]. Density functional theory (DFT) calculations at the B3LYP-D3(BJ)/6-311++G(2df,2p)//B3LYP/6-31+G(d,p) level of theory confirmed the proposed catalytic cycle. According to both experimental and DFT results, phosphate-assisted water nucleophilic attack to [(L)Co═O] played a key role in O-O bond formation.

Carbohydrates are diverse bio-macromolecules with highly complex structures that are involved in numerous biological processes. Well-defined carbohydrates obtained by chemical synthesis are essential to the understanding of their functions. However, synthesis of carbohydrates is greatly hampered by its insufficient efficiency. So far, assembly of long carbohydrate chains remains one of the most challenging tasks for synthetic chemists. Here we describe a highly efficient assembly of a 92-mer polysaccharide by the preactivation-based one-pot glycosylation protocol. Several linear and branched oligosaccharide/polysaccharide fragments ranging from 5-mer to 31-mer in length have been rapidly constructed in one-pot manner, which enables the first total synthesis of a biologically important mycobacterial arabinogalactan through a highly convergent [31+31+30] coupling reaction. Our results show that the preactivation-based one-pot glycosylation protocol may provide access to the construction of long and complicated carbohydrate chains.

Sterol O-acyltransferase 1 (SOAT1) is an endoplasmic reticulum (ER) resident, multitransmembrane enzyme that belongs to the membrane-bound O-acyltransferase (MBOAT) family. It catalyzes the esterification of cholesterol to generate cholesteryl esters for cholesterol storage. SOAT1 is a target to treat several human diseases. However, its structure and mechanism remain elusive since its discovery. Here, we report the structure of human SOAT1 (hSOAT1) determined by cryo-EM. hSOAT1 is a tetramer consisted of a dimer of dimer. The structure of hSOAT1 dimer at 3.5 Å resolution reveals that a small molecule inhibitor CI-976 binds inside the catalytic chamber and blocks the accessibility of the active site residues H460, N421 and W420. Our results pave the way for future mechanistic study and rational drug design targeting hSOAT1 and other mammalian MBOAT family members.

A new method for one-step construction of the tetracyclic core structure of the indole alkaloid (+)-minfiensine was developed utilizing a palladium-catalyzed asymmetric indole dearomatization/iminium cyclization cascade. An efficient total synthesis of (+)-minfiensine was realized using this strategy. The present method enables access to the common core structure of a series of monoterpene indole alkaloids, such as vincorine, echitamine, and aspidosphylline A.