Functionalization of Fe3O4/SiO2 with N-(2-Aminoethyl)-3-aminopropyl for Sorption of [AuCl4]-

Synthesis of Fe3O4/SiO2 modified with N-(2-aminoethyl)-3-aminopropyl group (Fe3O4/SiO2/ED) via coating method and its application for adsorption-desorption of anionic gold in aqueous solution have been conducted. The synthesized product was characterized with an X-ray diffractometer (XRD), a Fourier transform infrared (FT-IR) spectrophotometer and a transmission electron microscopy (TEM). Adsorption of Au(III) was conducted in a batch system and the variables included pH, contact time, and initial concentration were investigated. Results showed that magnetite/silica has been successfully functionalized with N-(2-aminoethyl)-3-aminopropyl in a homogeneous system. Kinetics study showed that adsorption of Au(III) followed the pseudo-second order model with rate constant of 0.710 g mmol L-1min-1. Furthermore, the experimental data fitted well with the Langmuir isotherm model with the maximum adsorption capacity for Au(III) of 142.9 mg g-1 and the energy of 25.0 kJ mol-1. Gold loaded on the Fe3O4/SiO2/ED could be easily desorbed with 0.2 mol L-1 HCl containing 2 wt.% of thiourea with recovery of 99.8%. Fe3O4/SiO2/ED was reusable and stable in 5 cycles of adsorption-desorption with recovery more than 90%. Fe3O4/SiO2/ED showed high selectivity towards Au(III) in the multimetal system Au(III)/Cu(II)/Cr(VI) with the coefficient selectivity for αAu-Cu of 227.5and for αAu-Cr of 12.3.

Crystal structure of thermospermine synthase from Medicago truncatula and substrate discriminatory features of plant aminopropyltransferases

Polyamines are linear polycationic compounds that play a crucial role in the growth and development of higher plants. One triamine (spermidine, SPD) and two tetraamine isomers (spermine, SPM, and thermospermine, TSPM) are obtained by the transfer of the aminopropyl group from decarboxylated S-adenosylmethionine to putrescine and SPD. These reactions are catalyzed by the specialized aminopropyltransferases. In that respect, plants are unique eukaryotes that have independently evolved two enzymes, thermospermine synthase (TSPS), encoded by the gene ACAULIS5, and spermine synthase, which produce TSPM and SPM, respectively. In this work, we structurally characterize the ACAULIS5 gene product, TSPS, from the model legume plant Medicago truncatula (Mt). Six crystal structures of MtTSPS — one without ligands and five in complexes with either reaction substrate (SPD), reaction product (TSPM), or one of three cofactor analogs (5′-methylthioadenosine, S-adenosylthiopropylamine, and adenosine) — give detailed insights into the biosynthesis of TSPM. Combined with small-angle X-ray scattering data, the crystal structures show that MtTSPS is a symmetric homotetramer with an interdomain eight-stranded β-barrel. Such an assembly and the presence of a hinge-like feature between N-terminal and C-terminal domains give the protein additional flexibility which potentially improves loading substrates and discarding products after the catalytic event. We also discuss the sequence and structural features around the active site of the plant aminopropyltransferases that distinguish them from each other and determine their characteristic substrate discrimination.

Maturation of the Translation Inhibitor Microcin C

ABSTRACT Microcin C (McC), an inhibitor of the growth of enteric bacteria, consists of a heptapeptide with a modified AMP residue attached to the backbone of the C-terminal aspartate through an N-acyl phosphamidate bond. Here we identify maturation intermediates produced by cells lacking individual mcc McC biosynthesis genes. We show that the products of the mccD and mccE genes are required for attachment of a 3-aminopropyl group to the phosphate of McC and that this group increases the potency of inhibition of the McC target, aspartyl-tRNA synthetase.

Oxidized polyamines and the growth of human vascular endothelial cells. Prevention of cytotoxic effects by selective acetylation

The responses of human umbilical-vein vascular endothelial cells in culture to the naturally occurring polyamines spermine, spermidine and putrescine, their acetyl derivatives and oxidation products were examined. In the absence of human polyamine oxidase, exposure of cells to polyamines (up to 160 microM) had no adverse effects. In the presence of polyamine oxidase, spermine and spermidine were cytotoxic, but putrescine was not. Acetylation of the aminopropyl group of spermidine or both aminopropyl groups of spermine prevented this cytotoxicity. The amino acids corresponding to the polyamines, representing a further stage of oxidation, were also without effect. The cytotoxic effects were irreversible. Use of bovine serum amine oxidase in place of the human enzyme gave qualitatively similar results.