On the Formation of Hydrogen Peroxide in Water Microdroplets

Abstract The aim of this work was to provide softwood kraft pulp fibres with new functionalities by the introduction of carbonyl groups. Carbonyl groups are known to affect properties such as wet strength through the formation of covalent bonds, i.e. hemiacetals. The method developed involves oxidation using hydrogen peroxide at mildly acidic conditions. It was found that the carbonyl group content increased with both increasing temperature and residence time when oxidized at acidic conditions. The number of carboxylic groups, however, remained approximately constant. There was virtually no increase in carbonyl groups when oxidation was performed at alkaline conditions. The maximum increase in carbonyl groups was found at a residence time of 90 min, a reaction temperature of 85 °C and a pH of 4. These conditions resulted in an increase in carbonyl groups from 30 to 122 µmol/g. When formed into a sheet, the pulp oxidized at acidic conditions proved to maintain its structural integrity at aqueous conditions. This indicates the formation of hemiacetal bonds between the introduced carbonyl groups and the hydroxyl groups on the carbohydrate chains. Thus, a possible application for the method could be fibre modification during the final bleaching stage of softwood kraft pulp, where the wet strength of the pulp could be increased.

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Mimicking catalase and catecholase enzymes by copper(II)-containing complexes

Open Chemistry ◽

10.1007/s11532-005-0009-6 ◽

2006 ◽

Vol 4 (1) ◽

pp. 118-134 ◽

Cited By ~ 5

Author(s):

István Szilágyi ◽

László. Horváth ◽

Imre Labádi ◽

Klara Hernadi ◽

István Pálinkó ◽

...

Keyword(s):

Hydrogen Peroxide ◽

Ion Exchange ◽

Silica Gel ◽

Catalase Activity ◽

Thermal Characteristics ◽

Hydrogen Peroxide Decomposition ◽

Covalent Bonds ◽

Peroxide Decomposition ◽

Catecholase Activity ◽

Ft Ir

AbstractAn imidazolate-bridged copper(II)-zinc(II) complex (Cu(II)-diethylenetriamino-μ-imidazolato-Zn(II)-tris(2-aminoethyl)amine perchlorate (denoted as “Cu,Zn complex”) and a simple copper(II) complex (Cu(II)-tris(2-aminoethyl) amine chloride (“Cu-tren”) were prepared and immobilised on silica gel (by hydrogen or covalent bonds) and montmorillonite (by ion exchange). The immobilised substances were characterised by FT-IR spectroscopy and their thermal characteristics were also studied. The obtained materials were tested in two probe reactions: catalytic oxidation of 3,5-di-tert-butyl catechol (DTBC) (catecholase activity) and the decomposition of hydrogen peroxide (catalase activity). It was found that the catecholase activity of the Cu,Zn complex increased considerably upon immobilization on silica gel via hydrogen bonds and intercalation by ion exchange among the layers of montmorillonite. The imidazolate-bridged copper(II)-zinc(II) complex and its immobilised versions were inactive in hydrogen peroxide decomposition. The Cu(II)-tris(2-aminoethyl)amine chloride complex displayed good catalase activity; however, immobilisation could not improve it.

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Electrochemical sensing of H2O2 released from living cells based on AuPd alloy-modified PDA nanotubes

Analytical Methods ◽

10.1039/c8ay02743a ◽

2019 ◽

Vol 11 (12) ◽

pp. 1651-1656 ◽

Cited By ~ 10

Author(s):

Guangli He ◽

Fengli Gao ◽

Wei Li ◽

Pengwei Li ◽

Xiaofan Zhang ◽

...

Keyword(s):

Hydrogen Peroxide ◽

Detection Method ◽

Living Cells ◽

Electrochemical Sensing ◽

Highly Efficient ◽

Efficient Detection ◽

Significant Attention

The highly efficient detection method for hydrogen peroxide (H2O2) has been attracting significant attention.

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Temperature Dependence of the Critical Electron Dose for Fatty Acid Monolayers

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100053188 ◽

1982 ◽

Vol 40 ◽

pp. 78-79

Author(s):

Kenneth H. Downing ◽

Robert M. Glaeser

Keyword(s):

Electron Beam ◽

Fatty Acid ◽

Inelastic Scattering ◽

Temperature Dependence ◽

Structural Damage ◽

Direct Result ◽

Second Step ◽

Strong Temperature Dependence ◽

Electron Dose ◽

Covalent Bonds

The structural damage of molecules irradiated by electrons is generally considered to occur in two steps. The direct result of inelastic scattering events is the disruption of covalent bonds. Following changes in bond structure, movement of the constituent atoms produces permanent distortions of the molecules. Since at least the second step should show a strong temperature dependence, it was to be expected that cooling a specimen should extend its lifetime in the electron beam. This result has been found in a large number of experiments, but the degree to which cooling the specimen enhances its resistance to radiation damage has been found to vary widely with specimen types.

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Peroxidase Localization in Hartmanella Trophozoites

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100065778 ◽

1971 ◽

Vol 29 ◽

pp. 346-347 ◽

Cited By ~ 1

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.

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Structural Transformation of a Germanium Σ=13 (510) [001] Tilt Grain Boundary under the Electron Beam

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100179014 ◽

1990 ◽

Vol 48 (1) ◽

pp. 52-53 ◽

Cited By ~ 1

Author(s):

Jean-Luc Rouvière ◽

Alain Bourret

Keyword(s):

Electron Microscopy ◽

High Resolution ◽

Grain Boundary ◽

Structural Transformation ◽

Mirror Symmetry ◽

High Resolution Electron Microscopy ◽

Structural Transformations ◽

Covalent Bonds ◽

Resolution Electron ◽

Tilt Grain Boundary

The possible structural transformations during the sample preparations and the sample observations are important issues in electron microscopy. Several publications of High Resolution Electron Microscopy (HREM) have reported that structural transformations and evaporation of the thin parts of a specimen could happen in the microscope. Diffusion and preferential etchings could also occur during the sample preparation.Here we report a structural transformation of a germanium Σ=13 (510) [001] tilt grain boundary that occurred in a medium-voltage electron microscopy (JEOL 400KV).Among the different (001) tilt grain boundaries whose atomic structures were entirely determined by High Resolution Electron Microscopy (Σ = 5(310), Σ = 13 (320), Σ = 13 (510), Σ = 65 (1130), Σ = 25 (710) and Σ = 41 (910), the Σ = 13 (510) interface is the most interesting. It exhibits two kinds of structures. One of them, the M-structure, has tetracoordinated covalent bonds and is periodic (fig. 1). The other, the U-structure, is also tetracoordinated but is not strictly periodic (fig. 2). It is composed of a periodically repeated constant part that separates variable cores where some atoms can have several stable positions. The M-structure has a mirror glide symmetry. At Scherzer defocus, its HREM images have characteristic groups of three big white dots that are distributed on alternatively facing right and left arcs (fig. 1). The (001) projection of the U-structure has an apparent mirror symmetry, the portions of good coincidence zones (“perfect crystal structure”) regularly separate the variable cores regions (fig. 2).

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

Biochemical Society Transactions ◽

10.1042/bst20200444 ◽

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.

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

Cell Biology International ◽

10.1042/cbi034s027d ◽

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

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Signal-regulated oxidation of proteins via MICAL

Biochemical Society Transactions ◽

10.1042/bst20190866 ◽

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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