Topic
Hydrogen peroxide
About: Hydrogen peroxide is a research topic. Over the lifetime, 42583 publications have been published within this topic receiving 1043732 citations. The topic is also known as: H2O2 & dioxidane.
Papers published on a yearly basis
Papers
More filters
TL;DR: In this paper, chemical and bactericidal effects induced by plasma in water upon electro-spraying through DC-driven positive transient spark discharge in air were investigated, and the degree of inactivation and oxidative damage of bacteria increased with the increasing acidity of the solution.
Abstract: Chemical and bactericidal effects induced by plasma in water upon electro-spraying through DC-driven positive transient spark discharge in air were investigated. Inactivation of E. coli was determined in dependence on pH (controlled by buffers) and correlated with chemical changes induced in water. Productions of hydrogen peroxide, nitrites, nitrates, peroxynitrites, and pH changes were determined, and the extent of oxidative stress induced in bacteria was evaluated. The degree of inactivation and oxidative damage of bacteria increased with the increasing acidity of the solution. Acidified nitrites interacting with hydrogen peroxide were determined as the most important bactericidal ROS/RNS agents in plasma-treated water. A possible role of peroxynitrites, ozone, and metal nanoparticles is discussed.
284 citations
TL;DR: Data indicate that flavonoids inhibit platelet function by blunting hydrogen peroxide production and, in turn, phospholipase C activation and suggest that the synergism among flavonoid could contribute to an understanding of the relation between the moderate consumption of red wine and the decreased risk of cardiovascular disease.
284 citations
TL;DR: Autoxidizing cysteine disrupts the integrity of hepatocytes causing release of glutathione, adenosine triphosphate and lactate dehydrogenase indicating that it is of little use as a therapeutic agent.
284 citations
TL;DR: This is the first report of a lignin peroxidase in a bacterium designated as ALiP-P3 and characterizations showed that this enzyme is a heme protein (Soret band, 408 nm) and a major component of the ligninolytic system of S. viridosporus T7A.
Abstract: Previously we reported production of an extracellular lignin-inducible peroxidase by Streptomyces viridosporus (M. Ramachandra, D.L. Crawford, and A.L. Pometto III, Appl. Environ. Microbiol. 53:2754-2760, 1987). This peroxidase was shown to oxidize 3,4-dihydroxyphenylalanine, 2,4-dichlorophenol, homoprotocatechuic acid, caffeic acid, and N,N,N',N'-tetramethylphenylenediamine and was found in higher than normal levels in strains enhanced for lignocellulose degradation. In the present study, we used a pure extracellular enzyme preparation with high peroxidase isoform P3 activity to oxidize lignin substructure model compounds of both the 1,2-diaryl propane and arylglycerol-beta-aryl ether types and containing C alpha-carbonyl and C alpha-hydroxyl groups. The reactions were monitored by gas chromatography-mass spectrometry and high-pressure liquid chromatography techniques. In the presence, but not the absence, of hydrogen peroxide, the enzyme preparation catalyzed C alpha-C beta bond cleavage in the side chains of the diaryl ethers 1-(3,4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1,3-diol (I) and 1-(4-hydroxy-3-methoxyphenyl)-2-(2-methoxyphenoxy)propan-1-one (II) and the diaryl ethane 1-(4-methoxyphenyl)-2-(phenyl)ethan-1-one (III). Rapid hydrogen peroxide consumption was observed when the enzyme preparation was added to either milled corn lignin or lignocellulose. Additional characterizations showed that this enzyme is a heme protein (Soret band, 408 nm) and a major component of the ligninolytic system of S. viridosporus T7A. This is the first report of a lignin peroxidase in a bacterium. We have designated this new lignin peroxidase as ALiP-P3.
284 citations
TL;DR: This analytical platform not only confirms the intrinsic peroxidase-like activity of the water-soluble cupric oxide nanoparticles, but also shows its great potential applications in environmental chemistry, biotechnology and medicine.
Abstract: Water-soluble cupric oxide nanoparticles are fabricated via a quick-precipitation method and used as peroxidase mimetics for ultrasensitive detection of hydrogen peroxide and glucose. The water-soluble CuO nanoparticles show much higher catalytic activity than that of commercial CuO nanoparticles due to their higher affinity to hydrogen peroxide. In addition, the as-prepared CuO nanoparticles are stable over a wide range of pH and temperature. This excellent stability in the form of aqueous colloidal suspensions makes the application of the water-soluble CuO nanoparticles easier in aqueous systems. A colorimetric assay for hydrogen peroxide and glucose has been established based on the catalytic oxidation of phenol coupled with 4-amino-atipyrine by the action of hydrogen peroxide. This analytical platform not only confirms the intrinsic peroxidase-like activity of the water-soluble cupric oxide nanoparticles, but also shows its great potential applications in environmental chemistry, biotechnology and medicine.
284 citations