Fast Reactions of Ascorbic Acid and Hydrogen Peroxide in Ice, a Presumptive Early Environment

Science ◽  
1965 ◽  
Vol 150 (3703) ◽  
pp. 1589-1590 ◽  
Author(s):  
N. H. Grant ◽  
H. E. Alburn
2019 ◽  
Vol 29 (3) ◽  
Author(s):  
Mai Ngọc Tuan Anh

Silver nanoplates (SNPs) having different size were synthesized by a seed-mediated method. The seeds -silver nanoparticles with 4 – 6 nm diameters were synthesized first by reducing silver nitrate with sodium borohydride in the present of Trisodium Citrate and Hydrogen peroxide. Then these seeds were developed by continue reducing Ag\(^+\) ions with various amount of L-Ascorbic acid to form SNPs. Our analysis showed that the concentratrion of L-Ascorbic acid, a secondary reducing agent, played an important role to form SNPs. In addition, the size and in-plane dipole plasmon resonance wavelenght of silver nanoplates were increased when the concentration of added silver nitrate increased. The characterization of SNPs were studied by UV-Vis, FE-SEM, EDS and TEM methods.


1991 ◽  
Vol 56 (4) ◽  
pp. 923-932
Author(s):  
Jana Stejskalová ◽  
Pavel Stopka ◽  
Zdeněk Pavlíček

The ESR spectra of peroxidase systems of methaemoglobin-ascorbic acid-hydrogen peroxide and methaemoglobin-haptoglobin complex-ascorbic acid-hydrogen peroxide have been measured in the acetate buffer of pH 4.5. For the system with methaemoglobin an asymmetrical signal with g ~ 2 has been observed which is interpreted as the perpendicular region of anisotropic spectrum of superoxide radical. On the other hand, for the system with methaemoglobin-haptoglobin complex the observed signal with g ~ 2 is symmetrical and is interpreted as a signal of delocalized electron. After realization of three repeatedly induced peroxidase processes the ESR signal of the perpendicular part of anisotropic spectrum of superoxide radical is distinctly diminished, whereas the signal of delocalized electron remains practically unchanged. An amino acid analysis of methaemoglobin along with results of the ESR measurements make it possible to derive a hypothesis about the role of haptoglobin in increasing of the peroxidase activity of methaemoglobin.


2008 ◽  
Vol 7 (11) ◽  
pp. 2008-2011 ◽  
Author(s):  
Olviyani Nasution ◽  
Kavitha Srinivasa ◽  
Minsun Kim ◽  
Yeo-Jung Kim ◽  
Wankee Kim ◽  
...  

ABSTRACT In this study, we demonstrate that hyphal differentiation is induced by the subtoxic concentration of exogenous H2O2 in Candida albicans. This finding is confirmed by the changing intracellular concentration of H2O2. In order to induce the same level of differentiation, low concentrations of exogenous H2O2 are required for the null mutants of the thiol-specific antioxidant and catalase, while higher concentrations are needed for cells treated with ascorbic acid, an antioxidant chemical.


2003 ◽  
Vol 69 (4) ◽  
pp. 2245-2252 ◽  
Author(s):  
J. B. Cross ◽  
R. P. Currier ◽  
D. J. Torraco ◽  
L. A. Vanderberg ◽  
G. L. Wagner ◽  
...  

ABSTRACT An approach to decontamination of biological endospores is discussed. Specifically, the performance of an aqueous modified Fenton reagent is examined. A modified Fenton reagent formulation of cupric chloride, ascorbic acid, and sodium chloride is shown to be an effective sporicide under aerobic conditions. The traditional Fenton reaction involves the conversion of hydrogen peroxide to hydroxyl radical by aqueous ionic catalysts such as the transition metal ions. Our modified Fenton reaction involves the conversion of aqueous dissolved oxygen to hydrogen peroxide by an ionic catalyst (Cu2+) and then subsequent conversion to hydroxyl radicals. Results are given for the modified Fenton reagent deactivating spores of Bacillus globigii. A biocidal mechanism is proposed that is consistent with our experimental results and independently derived information found in the literature. This mechanism requires diffusion of relatively benign species into the interior of the spore, where dissolved O2 is then converted through a series of reactions which ultimately produce hydroxyl radicals that perform the killing action.


2019 ◽  
Vol 31 (5) ◽  
pp. 851-857 ◽  
Author(s):  
Sayed Tayyab Raza Naqvi ◽  
Bahareh Shirinfar ◽  
Dilshad Hussain ◽  
Saadat Majeed ◽  
Muhammad Naeem Ashiq ◽  
...  

2014 ◽  
Vol 6 (20) ◽  
pp. 8321-8327 ◽  
Author(s):  
Kuo Chiang Lin ◽  
Jia Yan Huang ◽  
Shen Ming Chen

Illustration of electro-codeposition of PEDOT and FAD hybrid films using high conductivity and steric MWCNTs as a template.


In haemolysates of non-nucleated erythrocytes there is an inverse proportion between catalase activity and rate of choleglobin formation on addition of ascorbic acid. In the intact erythrocytes catalase protects haemoglobin against oxidation and further destruction by the hydrogen peroxide generated by the D-amino-acid oxidase system or by physiological concentrations of ascorbic acid and glutathione. Acid destromatization of haemolyzed horse erythrocytes causes a small decrease in the catalase activity and an increased rate of inactivation of the remaining catalase by ascorbic acid. The liberation of copper from haemocuprein is quantitatively insufficient to explain the decreased stability of the catalase. Exposing duck oxyhaemoglobin, but not reduced haemoglobin, to a pH of 5⋅5 to 5⋅8, causes an alteration which is apparent from the increase of the rate of choleglobin formation. The mechanism of this alteration is discussed. It partly explains the 'stroma effect', at least in duck erythrocytes. In addition, in the latter, there is a true stroma effect. Choleglobin formation in the presence of ascorbic acid is accelerated by a variety of substances. Some of these perturb haemoglobin, while others increase the formation of hydrogen peroxide from ascorbic acid. The implications of our findings on the mechanism of choleglobin formation and on the role of catalase in the erythrocyte are discussed.


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