Halide anions are formed from reactions between atomic metal anions and halogenated aromatic molecules.

Atomic metal anions (AMAs) Fe- , Cs- , Cu- and Ag- were generated in the gas phase by collisionally decomposing the corresponding metal-oxalate anion. Mass selected AMAs were allowed to react with halogenated and nitrated molecules (C6H5Cl, C6H4Cl2, C6H3Cl3, C6H5I, C6H5Br and C6H5NO2) in the collision hexapole of a triple-quadrupole mass spectrometer. Observed reactions include the predominant formation of X- (X = Cl, Br and I), as well as FeCl- , FeCl2- and FeCl3- when Fe- reacted with the mono, di and tri-chlorobenzenes; reactions between 1,4-dichlorobenzene and Cs- produced Cl- , CsCl- and CsCl2- ; reactions involving iodobenzene also produced, CsI- , CsI2- and AgI- . The results suggest that the reaction to form X- (X = Cl, Br, I and NO2) may be a promising route to improving the detection efficiency by mass spectrometry for such analytes. Copyright © 2016 John Wiley & Sons, Ltd.

Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2.

The SMYD (SET and MYND domain) family of lysine methyltransferases (KMTs) plays pivotal roles in various cellular processes, including gene expression regulation and DNA damage response. Initially identified as genuine histone methyltransferases, specific members of this family have recently been shown to methylate non-histone proteins such as p53, VEGFR, and the retinoblastoma tumor suppressor (pRb). To gain further functional insights into this family of KMTs, we generated the protein interaction network for three different human SMYD proteins (SMYD2, SMYD3, and SMYD5). Characterization of each SMYD protein network revealed that they associate with both shared and unique sets of proteins. Among those, we found that HSP90 and several of its co-chaperones interact specifically with the tetratrico peptide repeat (TPR)-containing SMYD2 and SMYD3. Moreover, using proteomic and biochemical techniques, we provide evidence that SMYD2 methylates K209 and K615 on HSP90 nucleotide-binding and dimerization domains, respectively. In addition, we found that each methylation site displays unique reactivity in regard to the presence of HSP90 co-chaperones, pH, and demethylation by the lysine amine oxidase LSD1, suggesting that alternative mechanisms control HSP90 methylation by SMYD2. Altogether, this study highlights the ability of SMYD proteins to form unique protein complexes that may underlie their various biological functions and the SMYD2-mediated methylation of the key molecular chaperone HSP90.