The efficient removal of alkyne impurities for the production of polymer-grade lower olefins remains an important and challenging goal for many industries. We report a strategy to control the pore interior of faujasite (FAU) zeolites by the confinement of isolated open nickel(II) sites in their six-membered rings. Under ambient conditions, Ni@FAU showed remarkable adsorption of alkynes and efficient separations of acetylene/ethylene, propyne/propylene, and butyne/1,3-butadiene mixtures, with unprecedented dynamic separation selectivities of 100, 92, and 83, respectively. In situ neutron diffraction and inelastic neutron scattering revealed that confined nickel(II) sites enabled chemoselective and reversible binding to acetylene through the formation of metastable [Ni(II)(C2H2)3] complexes. Control of the chemistry of pore interiors of easily scalable zeolites has unlocked their potential in challenging industrial separations.

Metal-organic framework MIL-53(Al) was explored as the stationary phase for high-performance liquid chromatographic separation of position isomers using a binary and/or polar mobile phase. Baseline separations of xylene, dichlorobenzene, chlorotoluene and nitrophenol isomers were achieved on the slurry-packed MIL-53(Al) column with high resolution and good precision. The effects of mobile phase composition, injected sample mass and temperature were investigated. The separation of xylene, dichlorobenzene, chlorotoluene and nitrophenol isomers on MIL-53(Al) were controlled by entropy change.

Metal-organic framework MIL-53(Al) is explored for reverse-phase high-performance liquid chromatographic separation of a wide range of analytes from non-polar to polar, and acidic to basic solutes with high resolution, good selectivity, stability and reproducibility.

Histone deacetylase 6 (HDAC6), a predominantly cytoplasmic protein deacetylase, participates in a wide range of cellular processes through its deacetylase activity. However, the diverse functions of HDAC6 cannot be fully elucidated with its known substrates. In an attempt to explore the substrate diversity of HDAC6, we performed quantitative proteomic analyses to monitor changes in the abundance of protein lysine acetylation in response to HDAC6 deficiency. We identified 107 proteins with elevated acetylation in the liver of HDAC6 knockout mice. Three cytoplasmic proteins, including myosin heavy chain 9 (MYH9), heat shock cognate protein 70 (Hsc70), and dnaJ homolog subfamily A member 1 (DNAJA1), were verified to interact with HDAC6. The acetylation levels of these proteins were negatively regulated by HDAC6 both in the mouse liver and in cultured cells. Functional studies reveal that HDAC6-mediated deacetylation modulates the actin-binding ability of MYH9 and the interaction between Hsc70 and DNAJA1. These findings consolidate the notion that HDAC6 serves as a critical regulator of protein acetylation with the capability of coordinating various cellular functions.Electronic supplementary materialThe online version of this article (doi:10.1007/s13238-014-0102-8) contains supplementary material, which is available to authorized users.