The oscillating reaction of Hydrogen Peroxide and Iodate with Butanone as substrate

1994 ◽  
Vol 26 (12) ◽  
pp. 1143-1150
Author(s):  
Ian Love
Keyword(s):  
Hydrogen Peroxide ◽  
Oscillating Reaction

Dynamic transitions in the Bray–Liebhafsky oscillating reaction. Effect of hydrogen peroxide and temperature on bifurcation

2016 ◽  
Vol 118 (1) ◽  
pp. 15-26 ◽  
Author(s):  
Nataša Pejić ◽  
Ljiljana Kolar-Anić ◽  
Jelena Maksimović ◽  
Marija Janković ◽  
Vladana Vukojević ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oscillating Reaction ◽  
Dynamic Transitions

scholarly journals Evidence of a Branched Chain Reaction in the Oscillating Reaction of Hydrogen Peroxide, Iodine, and Iodate.

1967 ◽  
Vol 21 ◽  
pp. 1057-1066 ◽  
Author(s):  
H. Degn ◽  
B.-O. Söderberg ◽  
C.-I. Brändén ◽  
Å. Åkeson ◽  
H. Theorell ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Chain Reaction ◽  
Oscillating Reaction ◽  
Branched Chain

Temperature-Induced Bifurcations in the Cu(II)-Catalyzed and Catalyst-Free Hydrogen Peroxide-Thiosulfate Oscillating Reaction

2010 ◽  
Vol 114 (26) ◽  
pp. 7014-7020 ◽  
Author(s):  
Ling Yuan ◽  
Qingyu Gao ◽  
Yuemin Zhao ◽  
Xiaodong Tang ◽  
Irving R. Epstein
Keyword(s):  
Hydrogen Peroxide ◽  
Catalyst Free ◽  
Free Hydrogen ◽  
Oscillating Reaction

A Study of the Cerium-catalyzed Briggs-Rauscher Oscillating Reaction

2012 ◽  
Vol 67 (1) ◽  
pp. 89-97 ◽  
Author(s):  
Stanley D. Furrow ◽  
Rinaldo Cervellati ◽  
Emanuela Greco
Keyword(s):  
Hydrogen Peroxide ◽  
Malonic Acid ◽  
Oscillatory Behavior ◽  
Concentration Change ◽  
Effective Catalyst ◽  
Low Concentrations ◽  
Oscillating Reaction ◽  
Leveling Effect

Cerium(III) catalysts can replace manganese(II) in the classic Briggs-Rauscher oscillator also containing acid, iodate, hydrogen peroxide, and malonic acid. H2SO4 was used as an acid; if HClO4 is used, cerium iodate precipitates. Cerium(III) oxalate typically precipitates by the time oscillations end. Ce(III) at low concentrations is roughly three times as effective asMn(II). At higher catalyst concentrations, there is a leveling effect for both. Oscillatory behavior with different concentrations is explored. Response to concentration change and inhibitors is similar with both catalysts. The mechanistic steps involving the catalysts must be similar. Ce(IV) is also an effective catalyst, although some cerium(IV) iodate may precipitate immediately.

scholarly journals The effect of Hydrogen Peroxide on a Chemical Oscillating Reaction.

2000 ◽  
Vol 16 (12) ◽  
pp. 1327-1330 ◽  
Author(s):  
Nanqin GAN ◽  
Ruxiu CAI ◽  
Zhixin LIN
Keyword(s):  
Hydrogen Peroxide ◽  
Oscillating Reaction

Peroxidase Localization in Hartmanella Trophozoites

1971 ◽  
Vol 29 ◽  
pp. 346-347 ◽  
Author(s):  
George E. Childs ◽  
Joseph H. Miller
Keyword(s):  
Hydrogen Peroxide ◽  
Ultrastructural Localization ◽  
Pathogenic Strain ◽  
Oxidative Enzymes ◽  
Differential Centrifugation ◽  
Electron Microscopic ◽  
Microscopic Studies ◽  
The Subject ◽  
Axenic Cultures

Biochemical and differential centrifugation studies have demonstrated that the oxidative enzymes of Acanthamoeba sp. are localized in mitochondria and peroxisomes (microbodies). Although hartmanellid amoebae have been the subject of several electron microscopic studies, peroxisomes have not been described from these organisms or other protozoa. Cytochemical tests employing diaminobenzidine-tetra HCl (DAB) and hydrogen peroxide were used for the ultrastructural localization of peroxidases of trophozoites of Hartmanella sp. (A-l, Culbertson), a pathogenic strain grown in axenic cultures of trypticase soy broth.

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.

Protective effect of chitooligosaccharides on hydrogen peroxide-induced PC-12 cells death by inhibition of oxidative damage

2010 ◽  
Vol 34 (8) ◽  
pp. S27-S27
Author(s):  
Xueling Dai ◽  
Ping Chang ◽  
Ke Xu ◽  
Changjun Lin ◽  
Hanchang Huang ◽  
...  
Keyword(s):  
Hydrogen Peroxide ◽  
Oxidative Damage ◽  
Protective Effect ◽  
Pc 12 Cells ◽  
Cells Death

Signal-regulated oxidation of proteins via MICAL

2020 ◽  
Vol 48 (2) ◽  
pp. 613-620
Author(s):  
Clara Ortegón Salas ◽  
Katharina Schneider ◽  
Christopher Horst Lillig ◽  
Manuela Gellert
Keyword(s):  
Signal Transduction ◽  
Hydrogen Peroxide ◽  
Cell Death ◽  
Redox Regulation ◽  
Signal Transduction Pathways ◽  
Cellular Functions ◽  
Intracellular Signals ◽  
Amino Acid Side Chains ◽  
Specific Receptors ◽  
Sulfur Containing

Processing of and responding to various signals is an essential cellular function that influences survival, homeostasis, development, and cell death. Extra- or intracellular signals are perceived via specific receptors and transduced in a particular signalling pathway that results in a precise response. Reversible post-translational redox modifications of cysteinyl and methionyl residues have been characterised in countless signal transduction pathways. Due to the low reactivity of most sulfur-containing amino acid side chains with hydrogen peroxide, for instance, and also to ensure specificity, redox signalling requires catalysis, just like phosphorylation signalling requires kinases and phosphatases. While reducing enzymes of both cysteinyl- and methionyl-derivates have been characterised in great detail before, the discovery and characterisation of MICAL proteins evinced the first examples of specific oxidases in signal transduction. This article provides an overview of the functions of MICAL proteins in the redox regulation of cellular functions.

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