Lizhi Tao

Hydroxyapatites (HAPm-T) of varying molar Ca/P ratios m (1.58–1.69) and calcination temperatures T (360–700 °C) were prepared and comprehensively characterized by nitrogen adsorption, TG, XPS, XRD, CO2-TPD, and NH3-TPD and were employed to catalyze the gas-phase dehydration of lactic acid (LA) to produce acrylic acid (AA). While the texture and crystallinity of the HAPm-T sample were affected little by variation of m, its surface acidity decreased but basicity increased with the increase in m. The HAPm-T sample with a higher T showed a higher crystallinity but lower surface area, acidity, and basicity. The conversion of LA decreased with increasing either m or T of the HAPm-T catalyst; the selectivity for AA maximized at m = 1.62 but decreased steadily with the T increase. The HAP1.62-360 sample (m = 1.62, T = 360 °C) was identified as the most efficient catalyst, offering an AA yield as high as 50–62% for longer than 8 h (AA selectivity: 71–74 mol %) under optimized reaction conditions (360 °C, WHSVLA= 1.4–2.1 h–1). Correlating the catalyst performance with its surface acidity and basicity disclosed that the LA consumption rate increased linearly with the acidity/basicity ratio, but volcano-type dependence appeared between the AA production rate and the acidity/basicity ratio, which reveals a kind of cooperative acid–base catalysis for selective AA production. The HAPm-T catalysts became more or less deactivated after reaction, but the reacted ones could be fully regenerated by in situ treatment with flowing air.

The bacterial manganese oxidase MnxG of the Mnx protein complex is unique among multicopper oxidases (MCOs) in carrying out a two-electron metal oxidation, converting Mn(II) to MnO2 nanoparticles. The reaction occurs in two stages: Mn(II) → Mn(III) and Mn(III) → MnO2. In a companion study, we show that the electron transfer from Mn(II) to the low-potential type 1 Cu of MnxG requires an activation step, likely forming a hydroxide bridge at a dinuclear Mn(II) site. Here we study the second oxidation step, using pyrophosphate (PP) as a Mn(III) trap. PP chelates Mn(III) produced by the enzyme and subsequently allows it to become a substrate for the second stage of the reaction. EPR spectroscopy confirms the presence of Mn(III) bound to the enzyme. The Mn(III) oxidation step does not involve direct electron transfer to the enzyme from Mn(III), which is shown by kinetic measurements to be excluded from the Mn(II) binding site. Instead, Mn(III) is proposed to disproportionate at an adjacent polynuclear site, thereby allowing indirect oxidation to Mn(IV) and recycling of Mn(II). PP plays a multifaceted role, slowing the reaction by complexing both Mn(II) and Mn(III) in solution, and also inhibiting catalysis, likely through binding at or near the active site. An overall mechanism for Mnx-catalyzed MnO2 production from Mn(II) is presented.

A copper-containing antibiotic Bacteria require transition metal ions for biological processes and must also protect themselves against excess metal, which is toxic. Patteson et al . explored how the environmental bacterium Pseudomonas aeruginosa uses a five-enzyme pathway to synthesize a small-molecule complex, fluopsin C, which is built from cysteine and contains a copper ion. The biosynthesis involves unusual enzymatic transformations that convert cysteine to a thiohydroximate, two of which chelate a copper ion in the final natural product. Fluopsin C protects P. aeruginosa from excess copper and also acts as a broad-spectrum antibiotic against other bacteria. —VV