Earth Abundant Oxidation Catalysts for Removal of Contaminants of Emerging Concern from Wastewater: Homogeneous Catalytic Screening of Monomeric Complexes.

Twenty novel Mn, Fe, and Cu complexes of ethylene cross-bridged tetraazamacrocycles with potentially copolymerizable allyl and benzyl pendant arms were synthesized and characterized. Multiple X-ray crystal structures demonstrate the cis-folded pseudo-octahedral geometry forced by the rigidifying ethylene cross-bridge and show that two cis coordination cites are available for interaction with substrate and oxidant. The Cu complexes were used to determine kinetic stability under harsh acidic and high-temperature conditions, which revealed that the cyclam-based ligands provide superior stabilization with half-lives of many minutes or even hours in 5 M HCl at 50-90 °C. Cyclic voltammetry studies of the Fe and Mn complexes reveal reversible redox processes indicating stabilization of Fe2+/Fe3+ and Mn2+/Mn3+/Mn4+ oxidation states, indicating the likelihood of catalytic oxidation for these complexes. Finally, dye-bleaching experiments with methylene blue, methyl orange, and rhodamine B demonstrate efficient catalytic decolorization and allow selection of the most successful monomeric catalysts for copolymerization to produce future heterogeneous water purification materials.

Synthesis and Characterization of Late Transition Metal Complexes of Mono-Acetate Pendant Armed Ethylene Cross-Bridged Tetraazamacrocycles with Promise as Oxidation Catalysts for Dye Bleaching.

Ethylene cross-bridged tetraazamacrocycles are known to produce kinetically stable transition metal complexes that can act as robust oxidation catalysts under harsh aqueous conditions. We have synthesized ligand analogs with single acetate pendant arms that act as pentadentate ligands to Mn, Fe, Co, Ni, Cu, and Zn. These complexes have been synthesized and characterized, including the structural characterization of four Co and Cu complexes. Cyclic voltammetry demonstrates that multiple oxidation states are stabilized by these rigid, bicyclic ligands. Yet, redox potentials of the metal complexes are modified compared to the "parent" ligands due to the pendant acetate arm. Similarly, gains in kinetic stability under harsh acidic conditions, compared to parent complexes without the pendant acetate arm, were demonstrated by a half-life seven times longer for the cyclam copper complex. Due to the reversible, high oxidation states available for the Mn and Fe complexes, the Mn and Fe complexes were examined as catalysts for the bleaching of three commonly used pollutant model dyes (methylene blue, methyl orange, and Rhodamine B) in water with hydrogen peroxide as oxidant. The efficient bleaching of these dyes was observed.

A novel peroxidase from runner bean (Phaseolus coccineus L.): Enhanced affinity purification, characterization, and dye decolorization activity.

In this study, a novel runner bean peroxidase (RBP) was purified and characterized. Affinity-based purification was performed with newly synthesized disubstituted 4-aminobenzohydrazides. In the purification results, 253-fold was achieved with a yield of 56.2%. Furthermore, molecular weight and enzyme purity were checked with the SDS-PAGE and observed a single band at 31.2 kDa. Optimum conditions were determined as temperature = 50°C, ionic strength = 0.2 M, and pH 7.0. Enzyme exhibited 31.2% of residual activity in the presence of 20% DMSO. Additionally, the redox-mediated decolorization effect of the enzyme was examined for Reactive Blue 19 and Acid Blue 25 dyes. As a result of 1-hr incubation, the enzyme removal activity of Reactive Blue 19 and Acid Blue 25 dyes was calculated as 47% and 57%, respectively. PRACTICAL APPLICATIONS: Peroxidases (PODs) ability to catalyze various redox reactions for many substrates makes them significant enzymes in industrial sectors. In our current report, a single-step strategy was developed and followed as an alternative to multi-step methods commonly used for the purification of PODs. During this process, high yield was achieved and the separation time was shortened. Also, the purification of RBP that can potentially supplant PODs used in the industrial applications was carried out for the first time. In addition, substrate specificity, catalytic behavior in water-miscible organic solvents, and dye bleaching activity of this enzyme have been determined to evaluate the utilization capacity in various processes.

Comparison between catalytic activities of two zinc layered hydroxide salts in brilliant green organic dye bleaching.

This paper reports the use of two layered hydroxide salts (LHS) (zinc hydroxide nitrate - ZHN - Zn5(OH)8(NO3)2·2H2O, and zinc hydroxide chloride - ZHC - Zn5(OH)8Cl2·H2O) as catalysts for brilliant green (BG) organic dye bleaching, using hydrogen peroxide as oxidant. The LHS were prepared by precipitation reaction between an aqueous solution of zinc salts and an aqueous ammonia solution. The solids were characterized by powder X-ray diffraction (XRD), electron paramagnetic resonance (EPR), ultraviolet-visible electronic spectroscopy (UV-Vis) and Fourier-transform infrared spectroscopy (FTIR). The catalytic activity of the solids was investigated at temperatures of 25, 35 and 45 °C, using different molar ratios of oxidant:dye:Zn2+ ions (present in the catalyst), in the absence and presence of ambient light. The kinetic aspect of the reaction was investigated considering that the reaction showed pseudo-first order behavior in relation to BG dye concentration. We propose a mechanism where superoxide radicals account for most of the bleaching taking place. The catalytic results obtained, along with the low cost and low toxicity of zinc compounds, establish ZHN and ZHC as novel catalysts for dye wastewater treatment, an area with constant demand for new methods and materials given its relationship with environmental equilibrium and human health.

Probing the Time Scale of FPOP (Fast Photochemical Oxidation of Proteins): Radical Reactions Extend Over Tens of Milliseconds.

Hydroxyl radical (⋅OH) labeling with mass spectrometry detection reports on protein conformations and interactions. Fast photochemical oxidation of proteins (FPOP) involves ⋅OH production via H2O2 photolysis by UV laser pulses inside a flow tube. The experiments are conducted in the presence of a scavenger (usually glutamine) that shortens the ⋅OH lifetime. The literature claims that FPOP takes place within 1 µs. This ultrafast time scale implies that FPOP should be immune to labeling-induced artifacts that may be encountered with other techniques. Surprisingly, the FPOP time scale has never been validated in direct kinetic measurements. Here we employ flash photolysis for probing oxidation processes under typical FPOP conditions. Bleaching of the reporter dye cyanine-5 (Cy5) served as readout of the time-dependent radical milieu. Surprisingly, Cy5 oxidation extends over tens of milliseconds. This time range is four orders of magnitude longer than expected from the FPOP literature. We demonstrate that the glutamine scavenger generates metastable secondary radicals in the FPOP solution, and that these radicals lengthen the time frame of Cy5 oxidation. Cy5 and similar dyes are widely used for monitoring the radical dose experienced by proteins in solution. The measured Cy5 kinetics thus strongly suggest that protein oxidation in FPOP extends over a much longer time window than previously thought (i.e., many milliseconds instead of one microsecond). The optical approach developed here should be suitable for assessing the performance of future FPOP-like techniques with improved temporal labeling characteristics. Graphical Abstract ᅟ.