Voltammetric studies of the interaction between lead metal ion and the methyl parathion pesticide

Cu-Mn alloy films are electrodeposited on Au substrates as precursor alloys for the synthesis of fine-structured nanoporous Cu structures. The alloys are deposited galvanostatically in a solution containing ammonium sulfate, (NH4)2SO4, which serves as a source of the ammine ligand that complexes with Cu, thereby decreasing the inherent standard reduction potential difference between Cu and Mn. The formation of the [Cu(NH3)n]2+ complex was confirmed by UV-Vis spectroscopic and voltammetric studies. Galvanostatic deposition at current densities ranging from 100 to 200 mA⋅cm−2 generally resulted in the formation of type I, crystalline coatings as revealed by scanning electron microscopy. Although the deposition current efficiency is (<30%) generally low, the atomic composition (determined by energy dispersive X-ray spectroscopy) of the deposited alloys range from 70–85 at% Mn, which is controlled by simply adjusting the ratio of the metal ion concentrations in the deposition bath. Anodic stripping characterization revealed a three-stage dissolution of the deposited alloys, which suggests control over the selective removal of Mn. The composition of the alloys obtained in the studies are ideal for electrochemical dealloying to form nanoporous Cu.

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Probing the mechanisms for the selectivity and promiscuity of methyl parathion hydrolase

Philosophical Transactions of The Royal Society A Mathematical Physical and Engineering Sciences ◽

10.1098/rsta.2016.0150 ◽

2016 ◽

Vol 374 (2080) ◽

pp. 20160150 ◽

Cited By ~ 14

Author(s):

Miha Purg ◽

Anna Pabis ◽

Florian Baier ◽

Nobuhiko Tokuriki ◽

Colin Jackson ◽

...

Keyword(s):

Transition State ◽

Metal Ions ◽

Metal Ion ◽

Methyl Parathion ◽

Model Systems ◽

Functional Evolution ◽

Methyl Parathion Hydrolase ◽

Wide Range ◽

Metal Metal ◽

Parathion Hydrolase

Diverse organophosphate hydrolases have convergently evolved the ability to hydrolyse man-made organophosphates. Thus, these enzymes are attractive model systems for studying the factors shaping enzyme functional evolution. Methyl parathion hydrolase (MPH) is an enzyme from the metallo-β-lactamase superfamily, which hydrolyses a wide range of organophosphate, aryl ester and lactone substrates. In addition, MPH demonstrates metal-ion-dependent selectivity patterns. The origins of this remain unclear, but are linked to open questions about the more general role of metal ions in functional evolution and divergence within enzyme superfamilies. Here, we present detailed mechanistic studies of the paraoxonase and arylesterase activities of MPH complexed with five different transition metal ions, and demonstrate that the hydrolysis reactions proceed via similar pathways and transition states. However, while it is possible to discern a clear structural origin for the selectivity between different substrates , the selectivity between different metal ions appears to lie instead in the distinct electrostatic properties of the metal ions themselves, which causes subtle changes in transition state geometries and metal–metal distances at the transition state rather than significant structural changes in the active site. While subtle, these differences can be significant for shaping the metal-ion-dependent activity patterns observed for this enzyme. This article is part of the themed issue ‘Multiscale modelling at the physics–chemistry–biology interface’.

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