Oxidative Decarboxylation Of Amino Acids Research Articles

Constructing Ultra-Strong SERS Tags in the Cellular Raman-Silent Region by Orthogonal Array Testing Strategy.

Surface-enhanced Raman spectroscopy (SERS) tags have the advantages of unique fingerprint vibration spectrum, ultranarrow spectral line widths, and weak photobleaching effect, showing great potential for bioimaging. However, SERS imaging is still hindered for further application due to its weak spontaneous Raman scattering, biomolecular signal interference, and long acquisition times. Here, we develop a novel SERS tag of the core (Au)-shell (N-doped graphene) structure (Au@NGs) with ultrastrong and stable Raman signal (2180 cm-1) in the cellular Raman-silent region (1800-2800 cm-1) through base-promoted oxidative decarboxylation of amino acids. Exploring the factors (metal salts, amino acids, catalysts, temperature, etc.) to obtain Au@NGs with the strongest Raman signal commonly requires more than 100,000 separate experiments, while that using an orthogonal array testing strategy is reduced to 56. The existence of deep charge transfer between the Au surface and C≡N-graphene is proved by theoretical calculations, which means the ultrastrong signal of Au@NGs is the joint effect of electromagnetic and chemical enhancement. The Au@NGs have a detection sensitivity down to a single-nanoparticle level, and high-speed and high-resolution cellular imaging (4453 pixels) is obtained within 10 s by global Raman imaging. The combination of Au@NGs-based tags with ultrastrong intrinsic Raman imaging capability and global imaging technology holds great promise for high-speed Raman imaging.

Synthetic Approaches to a Challenging and Unusual Structure—An Amino-Pyrrolidine Guanine Core

The synthesis of an unreported 2-aminopyrrolidine-1-carboxamidine unit is here described for the first time. This unusual and promising structure was attained through the oxidative decarboxylation of amino acids using the pair of reagents, silver(I)/peroxydisulfate (Ag(I)/S2O82−) followed by intermolecular (in the case of l-proline derivative) and intramolecular trapping (in the case of acyl l-arginine) by N-nucleophiles. The l-proline approach has a broader scope for the synthesis of 2-aminopyrrolidine-1-carboxamidine derivatives, whereas the intramolecular cyclization afforded by the l-acylarginines, when applied, results in higher yields. The former allowed the first synthesis of cernumidine, a natural alkaloid isolated in 2011 from Solanum cernuum Vell, as its racemic form.

Ruthenium-Catalyzed Oxidative Decarboxylation of Amino Acids

Ruthenium-Catalyzed Oxidative Decarboxylation of Amino Acids

Ruthenium-catalyzed aerobic oxidative decarboxylation of amino acids: a green, zero-waste route to biobased nitriles.

Oxidative decarboxylation of amino acids into nitriles was performed using molecular oxygen as terminal oxidant and a heterogeneous ruthenium hydroxide-based catalyst. A range of amino acids was oxidized in very good yield, using water as the solvent.

Bio-based nitriles from the heterogeneously catalyzed oxidative decarboxylation of amino acids.

The oxidative decarboxylation of amino acids to nitriles was achieved in aqueous solution by in situ halide oxidation using catalytic amounts of tungstate exchanged on a [Ni,Al] layered double hydroxide (LDH), NH4 Br, and H2 O2 as the terminal oxidant. Both halide oxidation and oxidative decarboxylation were facilitated by proximity effects between the reactants and the LDH catalyst. A wide range of amino acids was converted with high yields, often >90 %. The nitrile selectivity was excellent, and the system is compatible with amide, alcohol, and in particular carboxylic acid, amine, and guanidine functional groups after appropriate neutralization. This heterogeneous catalytic system was applied successfully to convert a protein-rich byproduct from the starch industry into useful bio-based N-containing chemicals.

Thermally induced oxidative decarboxylation of copper complexes of amino acids and formation of strecker aldehyde.

In the Maillard reaction, independent degradations of amino acids play an important role in the generation of amino-acid-specific products, such as Strecker aldehydes or their Schiff bases. Such oxidative decarboxylation reactions are expected to be enhanced in the presence of metals. Preliminary studies performed through heating of alanine and various metal salts (Cu, Fe, Zn, and Ca) under pyrolytic conditions indicated that copper(II) and iron(III) because of their high oxidation potentials were the only metals able to induce oxidative decarboxylation of amino acids and formation of Strecker aldehyde or its derivatives as detected by gas chromatography/mass spectrometry. Furthermore, studies performed with synthetic alanine and glycine copper complexes indicated that they constituted the critical intermediates undergoing free-radical oxidative degradation, followed by the loss of carbon dioxide and the generation of Strecker aldehydes, which were detected either as stable Schiff base adducts or incorporated in moieties, such as pyrazine or pyridine derivatives.

Optical sensing responses of CrIIICl(TPP)(H2O)-based coatings obtained by an atmospheric pressure plasma method – Application to the detection of volatile amines

Food spoilage processes are a considerable concern for both the food industry and the consumer, due to financial, food quality and food safety aspects. A primary issue is the prevention/monitoring of the formation of biogenic and volatile amines, such as occurring in fish and in other microbiologically unstable food items rich in proteins, produced by e.g. oxidative decarboxylation of amino acids. One strategy for their monitoring is the development of films with colorimetric sensing properties that are able to indicate food spoilage. The aim of this investigation was the development of a novel metalloporphyrin-based coating allowing the sensitive detection of typical volatile amines, such as trimethylamine (TMA), triethylamine (TEA) and dimethylamine (DMA), which were tested under static and dynamic flow conditions. Aqua(chloro)(5,10,15,20-tetraphenylporphyrinato)chromium(III) in solution at 0.75mgmL−1 was deposited by means of an atmospheric pressure dielectric barrier discharge deposition method onto 50μm thick transparent polyethylene terephthalate foils. Produced foils were able to detect volatile amines, as indicated via a hypsochromic shift of the Soret band of 5nm and differential absorption at 442nm, at 10ppm, while detectable static concentrations were higher (ca. 150ppm). Sensitivity was significantly higher for TMA, TEA and DMA than for NH3 (P<0.001), and sufficient humidity was a prerequisite for sensitive detection. Results were confirmed by experiments with spoiled fish (mackerel, trout). Further investigations of metalloporphyrins that could act as selective food spoilage indicators amenable to naked-eye detection are warranted.

Selective Oxidative Decarboxylation of Amino Acids to Produce Industrially Relevant Nitriles by Vanadium Chloroperoxidase

Industrial nitriles from biomass: Vanadium-chloroperoxidase is successfully used to transform selectively glutamic acid into 3-cyanopropanoic acid, a key intermediate for the synthesis of bio-succinonitrile and bio-acrylonitrile, by using a catalytic amount of a halide salt. This clean oxidative decarboxylation can be applied to mixtures of amino acids obtained from plant waste streams, leading to easily separable nitriles.

Oxidative decarboxylation of α-amino acids to nitriles using o-iodoxybenzoic acid in aqueous ammonia

Formation of the nitrile was the outcome of the investigation of biochemically significant oxidative decarboxylation of amino acids using o-iodoxybenzoic acid (IBX) in aqueous ammonia system.

Role of chloride in the oxidative decarboxylation of amino acids by chloramine-T

Role of chloride in the oxidative decarboxylation of amino acids by chloramine-T

Silver(I)/peroxydisulfate-induced oxidative decarboxylation of amino acids. A chemical model for a possible intermediate in the monoamine oxidase-catalyzed oxidation of amines

Silver(I)/peroxydisulfate-induced oxidative decarboxylation of amino acids. A chemical model for a possible intermediate in the monoamine oxidase-catalyzed oxidation of amines

Oxidative decarboxylation of amino acids by plant extracts

Oxidative decarboxylation of amino acids by plant extracts

Kinetics of Oxidative Decarboxylation of Amino Acids by Bromamine-T in Alkaline Medium

Kinetics of Oxidative Decarboxylation of Amino Acids by Bromamine-T in Alkaline Medium

Oxidation of branched-chain amino acids in skeletal muscle and liver of rat Effects of octanoate and energy state

The effect of octanoate on the oxidative decarboxylation of 14C-labeled amino acids has been studied in perfused hindquarter and liver of rat. Regulation of the branched-chain α-keto acid dehydrogenase has been further studied with α-[ 14C-1]ketoisovalerate in isolated rat muscle and liver mitochondria. (1) Octanoate has a stimulatory effect on the oxidation of branched-chain amino acids in perfused hindquarter. The oxidative decarboxylation of other amino acids are inhibited. Octanoate inhibits the oxidative decarboxylation of all amino acids in perfused liver. (2) The oxidation of valine is stimulated by octanoate and hexanoate also in isolated muscle mitochondria. The stimulatory effect is probably related to activation of the fatty acids since acyl-carnitines inhibit the oxidation. (3) The oxidation of α-ketoisovalerate in mitochondria is inhibited by competing substrates (pyruvate, α-ketoglutarate and succinate). This inhibition is counteracted by octanoate and ADP. (4) Low concentrations (1–5 μM) of 2,4-dinitrophenol (DNP) activates wheras higher concentrations inactivates the branched-chain α-keto acid dehydrogenase in intact but not in solubilized muscle mitochondria. The inactivation is counteracted by ATP, but is increased by octanoate. (5) The observations seem to suggest that the activation (like the inactivation) of branched-chain α-keto acid dehydrogenase in skeletal muscle is dependent on the mitochondrial energy state which therefore may regulate both activation and inactivation of the dehydrogenase.

Oxidative decarboxylation of free and peptide-linked amino acids in phagocytizing guinea pig granulocytes.

The oxidative decarboxylation of amino acids by a system consisting of myeloperoxidase-hydrogen peroxide-chloride has been demonstrated previously by others and the process has been considered to be part of the microbicidal armamentarium of some phagocytic leukocytes. We were able to translate these earlier observations, made on model systems, to intact guinea pig granulocytes. We could demonstrate differences in the cellular handling of peptide-linked amino acids as particles, compared with free amino acids. Specific inhibitors were used to explore two routes of oxidative decarboxylation: (a) the myeloperoxidase-catalyzed direct decarboxylation-deamination reaction, and (b) oxidation of alpha-keto acids after transamination of amino acids. These inhibitors were cyanide, azide, and tapazole for the former pathway, and amino-oxyacetate for the latter. Amino-oxyacetate profoundly inhibited the decarboxylation of free 14C-amino acids (alanine and aspartate) in both resting and stimulated cells, but had only a minimal effect on 14CO2 production from ingested insoluble 14C-protein. On the other hand, the peroxidase inhibitors cyanide, azide, and tapazole dramatically inhibited the production of 14CO2 from ingested particulate 14C-protein, but had only small effects on the decarboxylation of free amino acid. Soluble, uniformly labeled 14C-protein was not significantly converted to 14CO2 even in the presence of phagocytizable polystyrene beads. These observation suggest that the amino acids taken up by phagocytosis (e.g., as denatured protein particles) are oxidatively decarboxylated and deaminated in the phagosomes by the myeloperoxidase-hydrogen peroxide-chloride system; soluble free amino acids that enter the cytoplasm by diffusion or transport are oxidatively decarboxylated after transamination by the normal cellular amino acid oxidative pathway.