Enhancing gold recovery from electronic waste via lixiviant metabolic engineering in Chromobacterium violaceum

10.1038/srep02236Scientific Reports3

Lipophilic beta-adrenoceptor antagonists and local anesthetics are effective direct activators of G-proteins

We studied the effects of various beta-adrenoceptor (beta AR) antagonists and local anesthetics (LAs), i.e. substances possessing one basic and one lipophilic domain each, on activation of regulatory heterotrimeric guanine nucleotide-binding proteins (G-proteins). In membranes of differentiated HL-60 cells, propranolol activated high-affinity GTP hydrolysis with a half-maximal effect at 0.19 mM and a maximum at 1 mM. There was a close correlation between the log Q values (logarithm of the octanol: water partition coefficient) of beta AR antagonists and the logarithm of their effectiveness at activating GTPase (EC 3.6.1.-) in HL-60 membranes. The lipophilic LA, tetracaine, was also an effective activator of GTPase in HL-60 membranes, whereas more hydrophilic LAs were less stimulatory (bupivacaine and lidocaine) or even inhibitory (procaine). Propranolol and tetracaine also stimulated binding of guanosine 5'-O-[3-thio]triphosphate (GTP[gamma S]) to HL-60 membranes, but their stimulatory effects on GTP[gamma S] binding were smaller than on GTP hydrolysis. The stimulatory effects of propranolol and tetracaine on GTPase and GTP[gamma S] binding were inhibited by pertussis toxin. Propranolol and tetracaine effectively activated GTP hydrolysis of a reconstituted mixture of bovine brain Gi/Go-proteins, but the concentrations of substances needed for GTPase activation were higher than in HL-60 membranes. Procaine showed stimulatory effects on the GTPase of Gi/Go-proteins. Our data show that beta AR antagonists and LAs activate pertussis toxin-sensitive G-proteins, presumably through interaction with the C-terminus of their alpha-subunits. Apparently, the lipophilic domain of beta AR antagonists and LAs is more important for G-protein activation than the basic domain. We discuss the possibility that activation of nucleoside diphosphate kinase by beta AR antagonists and LAs contributes to their stimulatory effects on GTP hydrolysis in HL-60 membranes

The H1 receptor agonist 2-(3-chlorophenyl)histamine activates Gi proteins in HL-60 cells through a mechanism that is independent of known histamine receptor subtypes

In dibutyryl-cAMP-differentiated HL-60 cells, histamine H1 and formyl peptide receptors mediate increases in the cytosolic Ca2+ concentration ([Ca2+]i) via pertussis toxin-sensitive G proteins of the Gi family. We compared the effects of 2-(3-chlorophenyl)-histamine (CPH) [2-[2-(3-chlorophenyl)-1H-imidazol-4-yl] ethanamine], one of the most potent and selective H1 receptor agonists presently available, with those of histamine and N-formyl-L-methionyl-L-leucyl-L-phenylalanine (fMLP) in these cells. CPH increased [Ca2+]i through Ca2+ mobilization and Ca2+ influx. Unlike histamine-induced rises in [Ca2+]i, those induced by CPH were not desensitized in a homologous manner, and there was no cross-desensitization between CPH and histamine. Like fMLP, CPH activated phospholipases C and D, tyrosine phosphorylation, superoxide anion formation, and azurophilic granule release. The effects of CPH on [Ca2+]i, phospholipase D, and superoxide anion formation were inhibited by pertussis toxin. CPH and fMLP stimulated high affinity GTP hydrolysis by Gi proteins in HL-60 membranes. They also enhanced binding of guanosine-5'-O-(3-thio)triphosphate and GTP azidoanilide to, and cholera toxin-catalyzed ADP-ribosylation of, Gi protein alpha subunits. Histamine receptor antagonists did not inhibit the stimulatory effects of CPH, and CPH did not reduce fMLP binding in HL-60 membranes. Our data suggest that CPH activates Gi proteins in HL-60 cells through a receptor agonist-like mechanism that is, however, independent of known histamine receptor subtypes and formyl peptide receptors. CPH may be an agonist at an as yet unknown histamine receptor subtype or, by analogy with other cationic-amphiphilic substances, may activate G proteins directly. Future studies will have to take into consideration the fact that CPH, in addition to activating H1 receptors, may show other, most unexpected, stimulatory effects on G protein-mediated signal transduction processes

Leaching efficiency and kinetics of the recovery of palladium and rhodium from a spent auto-catalyst in HCl/CuCl2 media

The recycling of scarce elements such as platinum-group metals is becoming crucial due to their growing importance in current and emerging applications. In this sense, the recovery of palladium and rhodium from a spent auto-catalyst by leaching in HCl/CuCl2 media was studied, aiming at assessing the kinetic performance as well as the influence of some processing factors, and the behaviour of contaminant metals. Based on a kinetic model developed for the present case, the influence of temperature was evaluated and the corresponding values of activation energy were estimated as 60.1 ± 4.1 kJ mol-1 for Pd and 44.3 ± 7.3 kJ mol-1 for Rh, indicating the relevance of the chemical step rather than diffusion. This finding was corroborated by the non-significant influence of the stirring velocity. The reaction orders were estimated for each leaching reagent: for HCl, values of 2.1 ± 0.1 for Pd and 1.0 ± 0.3 for Rh were obtained; for Cu2+, the obtained values were 0.42 ± 0.04 for Pd and 0.36 ± 0.06 for Rh. Without any significant loss of efficiency, solutions with higher metal concentrations were obtained using lower liquid/solid ratios, such as 5 L/kg. The main contaminant in solution was aluminum, and its leaching was found to be very dependent on the temperature and acid concentration.Portuguese national funds through FCT – Fundação para a Ciência e a Tecnologia (Lisbon, Portugal), under the projects reference numbers PTDC/QUI-QUI/109970/2009, UID/Multi/04326/2019 and UID/MULTI/00612/2013.info:eu-repo/semantics/publishedVersio