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Time-programmable pH: decarboxylation of nitroacetic acid allows the time-controlled rising of pH to a definite value.

ABSTRACT: In this report it is shown that nitroacetic acid 1 (O₂NCH₂CO₂H) can be conveniently used to control the pH of a water solution over time. Time-programmable sequences of the kind pH_1(high)-pH_2(low)-pH_3(high) can be achieved, where both the extent of the initial pH jump (pH_1(high)-pH_2(low)) and the time required for the subsequent pH rising (pH_2(low)-pH_3(high)) can be predictably controlled by a judicious choice of the absolute and relative concentrations of the reagents (acid 1 and NaOH). Successive pH_1(high)-pH_2(low)-pH_3(high) sequences can be obtained by subsequent additions of acid 1. As a proof of concept, the method is applied to control over time the pH-dependent host-guest interaction between alpha-cyclodextrin and p-aminobenzoic acid.

SUBMITTER: Del Giudice D

PROVIDER: S-EPMC8171335 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature

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Time-programmable pH: decarboxylation of nitroacetic acid allows the time-controlled rising of pH to a definite value.

Del Giudice Daniele D Spatola Emanuele E Valentini Matteo M Bombelli Cecilia C Ercolani Gianfranco G Di Stefano Stefano S

Chemical science 20210421 21

In this report it is shown that nitroacetic acid 1 (O2NCH2CO2H) can be conveniently used to control the pH of a water solution over time. Time-programmable sequences of the kind pH1(high)-pH2(low)-pH3(high) can be achieved, where both the extent of the initial pH jump (pH1(high)-pH2(low)) and the time required for the subsequent pH rising (pH2(low)-pH3(high)) can be predictably co ...[more]

PMID: 34163836

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Project description:Plant aromatic amino acid decarboxylase (AAAD) enzymes are capable of catalyzing either decarboxylation or decarboxylation-deamination on various combinations of aromatic amino acid substrates. These two different activities result in the production of arylalkylamines and the formation of aromatic acetaldehydes, respectively. Variations in product formation enable individual enzymes to play different physiological functions. Despite these catalytic variations, arylalkylamine and aldehyde synthesizing AAADs are indistinguishable without protein expression and characterization. In this study, extensive biochemical characterization of plant AAADs was performed to identify residues responsible for differentiating decarboxylation AAADs from aldehyde synthase AAADs. Results demonstrated that a tyrosine residue located on a catalytic loop proximal to the active site of plant AAADs is primarily responsible for dictating typical decarboxylase activity, whereas a phenylalanine at the same position is primarily liable for aldehyde synthase activity. Mutagenesis of the active site phenylalanine to tyrosine in Arabidopsis thaliana and Petroselinum crispum aromatic acetaldehyde synthases primarily converts the enzymes activity from decarboxylation-deamination to decarboxylation. The mutation of the active site tyrosine to phenylalanine in the Catharanthus roseus and Papaver somniferum aromatic amino acid decarboxylases changes the enzymes decarboxylation activity to a primarily decarboxylation-deamination activity. Generation of these mutant enzymes enables the production of unusual AAAD enzyme products including indole-3-acetaldehyde, 4-hydroxyphenylacetaldehyde, and phenylethylamine. Our data indicates that the tyrosine and phenylalanine in the catalytic loop region could serve as a signature residue to reliably distinguish plant arylalkylamine and aldehyde synthesizing AAADs. Additionally, the resulting data enables further insights into the mechanistic roles of active site residues.

Dataset Information

Time-programmable pH: decarboxylation of nitroacetic acid allows the time-controlled rising of pH to a definite value.

Publications

Time-programmable pH: decarboxylation of nitroacetic acid allows the time-controlled rising of pH to a definite value.

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