A Kinetic Study of the Oxidation of Mercaptans Catalyzed by Hydroquinone and its Homologs

Meguerian, G. H.

doi:10.1021/ja01624a025

Cited by 12 publications

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“…The apparent inactivation of menadione is also of interest in view of evidence that mercaptans in excess, in the presence of oxygen, may convert quinones to di-, tri-and tetramercaptoquinones (Meguerian, 1955). Such reactions between cellular sulphydryl groups and menadione might well be the cause of the gradual loss of catalytic activity.…”

Section: Attempt To Elucidate the Decreasing Effect Of Msnadione Withmentioning

confidence: 99%

The Effect of Menadione on the Reduction of Methaemoglobin

Harley¹,

Robin²

1962

Aust J Exp Biol Med

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SUMMARY.The effect of menadione on the reduction of methaemoglobin by normal and gIueose-6-phosphate dehydrogenase-deficient (G6PD-dcficient) human erythrocytes has been studied. With ghicose as substrate, menadione cansed an increased rate of methaemoglobin reduction in normal but not in G6PD-deficient erythrocytes. With laetate, menadione produced enhanced methaemoglobin reduction in both normal and G6PD-deficient erythrocytes.The effect of menadfone appeared somewhat similar in nature to that produced by methylene blue, but of lesser degree and shorter duration. Evidence was presented to show that menadione-induced methaemoglobin formation may complicate the kinetics of methaemoglobin reduction, particularly with higher concentrations of menadione and lower initial concentrations of methaemoglobin.It was suggested that menadione enhances the reduction of methaemoglobin mainly by catalysing reduced nicotinamide-adenine dinucleotide phosphate-dependent reduction of methaemoglobin, but also under certain circumstances by stimulating one or more reduced nicotinamide-adenine dinucleotide-dependent pathways of methaemoglobin reduction.INTRODUCTION.

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Section: Attempt To Elucidate the Decreasing Effect Of Msnadione Withmentioning

confidence: 99%

The Effect of Menadione on the Reduction of Methaemoglobin

Harley¹,

Robin²

1962

Aust J Exp Biol Med

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“…[1,6,[16][17][18][19][20][21][22] In organic media, thiols are oxidized into disulfides by oxygen from the air,c atalyzed by heavy metal ions, [1,16] metal nanoparticles, [17] or other organic catalysts. [18,19] Furthermore, this coupling has also been achieved by the redox reactiono ft hiols with oxidants such as iodine [20] and graphene oxide. [21] In aqueous media, aerobic oxidative coupling can be easily conducted in alkalines olution.…”

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Polydopamine as a Catalyst for Thiol Coupling

Yang

et al. 2015

ChemCatChem

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In biological systems, disulfide bonds are formed efficiently under mild conditions without the release of harmful byproducts. Inspired by nature, we report a biomimetic polydopamine (PDA) catalyst for oxidative thiol coupling. This reaction was accelerated with only a small amount of PDA particles in neutral, weakly alkaline, and even weakly acidic aqueous media at room temperature under an air atmosphere. The catalytic particles were facilely separated and were reused without a decrease in activity. The entire process is totally biofriendly, including the synthesis of the PDA particles. This route is especially useful for the synthesis of pharmaceutical molecules.

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Detection and Quantitation of Biological Sulfhydryls

Russo

Bump

1988

Methods of Biochemical Analysis

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A Kinetic Study of the Oxidation of Mercaptans Catalyzed by Hydroquinone and its Homologs

Cited by 12 publications

References 1 publication

The Effect of Menadione on the Reduction of Methaemoglobin

The Effect of Menadione on the Reduction of Methaemoglobin

Polydopamine as a Catalyst for Thiol Coupling

Detection and Quantitation of Biological Sulfhydryls

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