Decarboxylation

About: Decarboxylation is a research topic. Over the lifetime, 9914 publications have been published within this topic receiving 193955 citations. The topic is also known as: decarboxylation reaction.

Acrylamide formation mechanism in heated foods.

Abstract: Recent findings of a potential human carcinogen, acrylamide, in foods have focused research on the possible mechanisms of formation. We present a mechanism for the formation of acrylamide from the reaction of the amino acid asparagine and a carbonyl-containing compound at typical cooking temperatures. The mechanism involves formation of a Schiff base followed by decarboxylation and elimination of either ammonia or a substituted imine under heat to yield acrylamide. Isotope substitution studies and mass spectrometric analysis of heated model systems confirm the presence of key reaction intermediates. Further confirmation of this mechanism is accomplished through selective removal of asparagine with asparaginase that results in a reduced level of acrylamide in a selected heated food.

Direct identification of the calcium-binding amino acid, gamma-carboxyglutamate, in mineralized tissue

Abstract: A direct approach has been developed for quantitative identification of the calcium-binding amino acid, gamma-carboxyglutamate, in proteins. This should be advantageous for the study of numerous systems where specific roles for the binding of calcium or other divalent cations are suspected. Investigation of mineralized tissue, where calcium-binding proteins are implicated in the mineralization process, revealed that gamma-carboxyglutamate was present in proteins solubilized from chicken bone with neutral aqueous ethylenediamine tetraacetic acid. This was established by direct isolation of the amino acid from alkaline hydrolysates and its quantitative conversion to glutamic acid by decarboxylation in 0.05 M HCl at 100 degrees. The kinetics of decarboxylation and chromatographic behavior are identical to those of gamma-carboxyglutamate from human prothrombin. After resolution of the soluble bone proteins by phosphate gradient elution from hydroxyapatite, gamma-carboxyglutamate was found to be concentrated primarily in one BaSO4-adsorbable anionic protein species; bone collagen was devoid of the amino acid. In view of the recently discovered requirement of vitamin K for generation of calcium binding sites (gamma-carboxyglutamate) by gamma-carboxylation of specific glutamic acid residues in prothrombin, our findings may implicate vitamin K metabolism in normal bone development and suggest a role for the gamma-carboxyglutamate-rich protein in regulation of calcium salt deposition in mineralized tissues.

Discriminating between the six isomers of dicaffeoylquinic acid by LC-MS^n

Abstract: The fragmentation behavior of all six dicaffeoylquinic acids (diCQA) has been investigated using LC-MS(4). It is possible to discriminate between each of the isomers including those for which commercial standards are not available. For diCQA, the ease of removal of the caffeoyl residue during fragmentation is 1 approximately = 5 > 3 > 4. The distinctive fragmentation observed for the little-studied 1,4-dicaffeoylquinic acid involves elimination of the C1 caffeoyl residue, repeated dehydrations leading to the aromatization of the quinic acid moiety, and its decarboxylation. It is suggested that this process is initiated by the C1 carboxyl protonating the C5 hydroxyl in the inverted chair conformer, followed by its protonating the C1 caffeoyl residue in the favored chair conformation. The fragmentation of 1-caffeoylquinic acid is indistinguishable from that of the commercially available 5-caffeoylquinic acid, but these two isomers can be distinguished easily by their facile chromatographic resolution on reversed phase packings. The hierarchical key previously developed for characterizing chlorogenic acids has been extended to accommodate 1-caffeoylquinic acid and the 1-acyl dicaffeoylquinic acids.

The First Direct Characterization of a High-Valent Iron Intermediate in the Reaction of an α-Ketoglutarate-Dependent Dioxygenase: A High-Spin Fe(IV) Complex in Taurine/α-Ketoglutarate Dioxygenase (TauD) from Escherichia coli†

Abstract: The Fe(II)- and α-ketoglutarate(αKG)-dependent dioxygenases have roles in synthesis of collagen and sensing of oxygen in mammals, in acquisition of nutrients and synthesis of antibiotics in microbes, and in repair of alkylated DNA in both. A consensus mechanism for these enzymes, involving (i) addition of O2 to a five-coordinate, (His)2(Asp)-facially coordinated Fe(II) center to which αKG is also bound via its C-1 carboxylate and ketone oxygen; (ii) attack of the uncoordinated oxygen of the bound O2 on the ketone carbonyl of αKG to form a bicyclic Fe(IV)-peroxyhemiketal complex; (iii) decarboxylation of this complex concomitantly with formation of an oxo-ferryl (Fe(IV)O2-) intermediate; and (iv) hydroxylation of the substrate by the Fe(IV)O2- complex via a substrate radical intermediate, has repeatedly been proposed, but none of the postulated intermediates occurring after addition of O2 has ever been detected. In this work, an oxidized Fe intermediate in the reaction of one of these enzymes, taurine/α-ke...