63296-34-4Relevant academic research and scientific papers
Flavonoids as promoters of the (pseudo-)halogenating activity of lactoperoxidase and myeloperoxidase
Gau, Jana,Furtmüller, Paul G.,Obinger, Christian,Prévost, Martine,Van Antwerpen, Pierre,Arnhold, Jürgen,Flemmig, J?rg
, p. 307 - 319 (2016)
In this study several flavonoids were tested for their potential to regenerate the (pseudo-)halogenating activity (hypothiocyanite formation) of the heme peroxidases lactoperoxidase (LPO) and myeloperoxidase (MPO) after hydrogen peroxide-mediated enzyme inactivation. Several flavonoid subclasses with varying hydroxylation patterns (especially of the flavonoid B-ring) were examined in order to identify structural properties of efficient enzyme regenerators. Kinetic parameters and second-order rate constants were determined. A 3′,4′-dihydroxylated B-ring together with C-ring saturation and hydroxylation were found to be important structural elements, which strongly influence the flavonoid binding and oxidizability by the LPO/MPO redox intermediates Compounds I and II. In combination with docking studies these results allow an understanding of the differences between flavonoids that promote the hypothiocyanite production by LPO and MPO and those that inhibit this enzymatic reaction.
On Electrochemical oxidation of thiocyanates in solutions for cyanidation of gold-containing ores and concentrates
Kenova,Kormienko,Drozdov
, p. 1589 - 1592 (2010)
Effect of hydrogen peroxide on the electrochemical oxidation of thiocyanate-containing solutions was studied.
Redox buffering of hypochlorous acid by thiocyanate in physiologic fluids
Ashby, Michael T.,Carlson, Amy C.,Scott, M. Jared
, p. 15976 - 15977 (2004)
The major antimicrobial products of neutrophilic myeloperoxidase (MPO) in physiologic fluids are hypochlorous acid (HOCl) and hypothiocyanite (OSCN-), and the former is generally believed to be the killing agent. However, we have determined that HOCl oxidizes SCN- in a facile nonenzymic reaction. The observed kinetics and computational models substantiate the hypothesis that SCN- serves to moderate the potential autotoxicity of HOCl by restricting its lifetime in physiologic fluids. Furthermore, the oxidizing equivalents of HOCl are preserved in OSCN-, a more discriminate biocide that is not lethal to mammalian cells. Copyright
Detailed kinetics and mechanism of the oxidation of thiocyanate ion (SCN-) by peroxomonosulfate ion (HSO5-). Formation and subsequent oxidation of hypothiocyanite ion (OSCN-)
Kalmár, József,Lente, Gábor,Fábián, István
, p. 2150 - 2156 (2013/03/28)
The haloperoxidase-catalyzed in vivo oxidation of thiocyanate ion (SCN -) by H2O2 is important for generation of the antimicrobial hypothiocyanite ion (OSCN-), which is also susceptible to oxidation by strong in vivo oxidizing agents (i.e., H2O 2, OCl-, OBr-). We report a detailed mechanistic investigation on the multistep oxidation of excess SCN- with peroxomonosulfate ion (HSO5- in the form of Oxone) in the range from pH 6.5 to 13.5. OSCN- was detected to be the intermediate of this reaction under the above conditions, and a kinetic model is proposed. Furthermore, by kinetic separation of the consecutive reaction steps, the rate constant of the direct oxidation of OSCN- by HSO 5- was determined: k2 = (1.6 ± 0.1) × 102 M-1 s-1 at pH 13.5 and k 2H = (3.3 ± 0.1) × 103 M -1 s-1 at pH 6.89. A critical evaluation of the estimated activation parameters of the elementary steps revealed that the oxidations of SCN- as well as the consecutive OSCN- by HSO 5- are more likely to proceed via 2e--transfer steps rather than 1e- transfer.
