Use of Screen-printed Electrodes Modified by Prussian Blue and Analogues in Sensing of Cysteine

© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim The utilisation of screen-printing technology allows for a mass scalable approach for the production of electrochemical screen-printed electrodes (SPEs) and the presence of a redox mediator can add new possibilities to the electrochemical properties of the SPEs. Among the materials used as redox mediators, cyanidoferrates polymers can be used for electro-oxidation of cysteine. In this work, two monomers, namely, [Fe(CN) 6 ] 4− and [Fe(CN) 5 NH 3 ] 3− were used to produce Prussian blue (PB) and Prussian blue-Ammine (PB-Ammine), respectively. In addition, two modification methods were compared, firstly via a drop-casting and secondly by the incorporation of these materials into a printable ink. The SPE modified by PB-Ammine (drop-casting) exhibits the highest electroactive area, however the highest heterogeneous rate constant was found with the SPE modified by PB-Ammine that was incorporated into the ink. The highest value of the constant of electro-oxidation of cysteine and lowest limit of detection was also observed in the SPE modified by PB incorporated into the ink. These studies suggest that the electrocatalytic properties of SPE modified by PB and PB-Ammine are dependent upon the availability of Fe 3+ catalytic sites and the increased kinetics of the chemical reaction between the catalytic sites and the analyte

Ni−Fe (Oxy)hydroxide Modified Graphene Additive Manufactured (3D-Printed) Electrochemical Platforms as an Efficient Electrocatalyst for the Oxygen Evolution Reaction

© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim We demonstrate that polylactic acid (PLA)/graphene additive manufactured (3D-printed) electrodes (Gr/AMEs) electrodeposited with Ni−Fe (oxy)hydroxide can efficiently catalyse the oxygen evolution reaction (OER). X-ray photoelectron spectroscopy (XPS) depth profiling combined with Atomic Force Microscopy (AFM) and Tip Enhanced Raman Spectroscopy (TERS) deduced the composition and depth of the Ni−Fe (oxy)hydroxide layer. The composition of the resulting electrocatalytic surfaces are tailored through altering the concentrations of nickel and iron within the electrodeposited solutions, which give rise to optimised AMEs OER performance (within 0.1 M KOH). The optimal OER performance was observed from a Ni−Fe (oxy)hydroxide with a 10 % content of Fe, which displayed an OER onset potential and overpotential of+1.47 V (vs. RHE) and 519 mV, respectively. These values arecomparable to that of polycrystalline Iridium (+ 1.43 V (vs. RHE) and ca. 413 mV), as well as being significantly less electropositive than a bare/unmodified AME. This work is essential for those designing, fabricating and modulating additive manufactured electrodes

The yeast P5 type ATPase, Spf1, regulates manganese transport into the endoplasmic reticulum

The endoplasmic reticulum (ER) is a large, multifunctional and essential organelle. Despite intense research, the function of more than a third of ER proteins remains unknown even in the well-studied model organism Saccharomyces cerevisiae. One such protein is Spf1, which is a highly conserved, ER localized, putative P-type ATPase. Deletion of SPF1 causes a wide variety of phenotypes including severe ER stress suggesting that this protein is essential for the normal function of the ER. The closest homologue of Spf1 is the vacuolar P-type ATPase Ypk9 that influences Mn2+ homeostasis. However in vitro reconstitution assays with Spf1 have not yielded insight into its transport specificity. Here we took an in vivo approach to detect the direct and indirect effects of deleting SPF1. We found a specific reduction in the luminal concentration of Mn2+ in ∆spf1 cells and an increase following it’s overexpression. In agreement with the observed loss of luminal Mn2+ we could observe concurrent reduction in many Mn2+-related process in the ER lumen. Conversely, cytosolic Mn2+-dependent processes were increased. Together, these data support a role for Spf1p in Mn2+ transport in the cell. We also demonstrate that the human sequence homologue, ATP13A1, is a functionally conserved orthologue. Since ATP13A1 is highly expressed in developing neuronal tissues and in the brain, this should help in the study of Mn2+-dependent neurological disorders