Peroxy Compounds, Organic

Klenk, Herbert; Götz, Peter; Siegmeier, R.; Mayr, W.

doi:10.1002/14356007.a19_199

Cited by 27 publications

(26 citation statements)

References 265 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For this reason, KatG can, at least in theory, detoxify other peroxide compounds, for example, peroxy acids and peroxy lipids quickly produced as the result of H 2 O 2 exposure. It has been reported that H 2 O 2 can directly oxidize a variety of cellular components, including DNA, protein, lipid and various cellular organelles [20, 41] as well as common metabolites such as carboxylic acids [18]. It is plausible that through such a mechanism KatG, but not KatE, is able to detoxify the peroxy compounds generated by H 2 O 2 and confer cells resistance to H 2 O 2 .…”

Section: Discussionmentioning

confidence: 99%

KatG and KatE confer Acinetobacter resistance to hydrogen peroxide but sensitize bacteria to killing by phagocytic respiratory burst

et al. 2016

View full text Add to dashboard Cite

Aims Catalase catalyzes the degradation of H2O2. Acinetobacter species have four predicted catalase genes, katA, katE, katG, and katX. The aims of the present study seek to determine which catalase(s) plays a predominant role in determining the resistance to H2O2, and to assess the role of catalase in Acinetobacter virulence. Main Methods Mutants of A. baumannii and A. nosocomialis with deficiencies in katA, katE, katG, and katX were tested for sensitivity to H2O2, either by halo assays or by liquid culture assays. Respiratory burst of neutrophils, in response to A. nosocomialis, was assessed by chemiluminescence to examine the effects of catalase on the production of reactive oxygen species (ROS)1 in neutrophils. Bacterial virulence was assessed using a Galleria mellonella larva infection model. Key findings The capacities of A. baumannii and A. nosocomialis to degrade H2O2 are largely dependent on katE. The resistance of both A. baumannii and A. nosocomialis to H2O2 is primarily determined by the katG gene, although katE also plays a minor role in H2O2 resistance. Bacteria lacking both the katG and katE genes exhibit the highest sensitivity to H2O2. While A. nosocomialis bacteria with katE and/or katG were able to decrease ROS production by neutrophils, these cells also induced a more robust respiratory burst in neutrophils than did cells deficient in both katE and katG. We also found that A. nosocomialis deficient in both katE and katG was more virulent than the wildtype A. nosocomialis strain. Significance Our findings suggest that inhibition of Acinetobacter catalase may help to overcome the resistance of Acinetobacter species to microbicidal H2O2 and facilitate bacterial disinfection.

show abstract

Section: Discussionmentioning

confidence: 99%

KatG and KatE confer Acinetobacter resistance to hydrogen peroxide but sensitize bacteria to killing by phagocytic respiratory burst

et al. 2016

View full text Add to dashboard Cite

show abstract

“…Peracids may be decomposed at alkaline pHs. The mechanism of peracid decomposition results in the formation of highly reactive singlet molecular oxygen [19].…”

Section: Discussionmentioning

confidence: 99%

“…Simulations were performed for dianionic phosphotyrosine, while the C4, C8 and C12 peracids, having pK a 's in the range of 8.1-10.8 [19], were modeled in both neutral and anionic forms. The structures obtained by molecular docking were used as input for the molecular dynamics simulations.…”

Section: Molecular Dynamicsmentioning

confidence: 99%

“…Peracids are highly reactive (Fig. 1C) and are therefore more potent oxidants than hydrogen peroxide [19]. It has been shown that peracetic acid (C2-peracid), likely formed in chronic alcoholics from acetic acid and hydrogen peroxide, may inhibit enzyme that contains thiol groups, arachidonoyl-CoA: 1-palmitoyl-sn-glycero-3-phosphocholine acyl transferase, localized in the erythrocyte membrane [20].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Inactivation of Protein Tyrosine Phosphatases by Peracids Correlates with the Hydrocarbon Chain Length

Kuban–Jankowska

Górska

Tuszyński

et al. 2015

Cell Physiol Biochem

View full text Add to dashboard Cite

Background/Aims: Protein tyrosine phosphatases are crucial enzymes controlling numerous physiological and pathophysiological events and can be regulated by oxidation of the catalytic domain cysteine residue. Peracids are highly oxidizing compounds, and thus may induce inactivation of PTPs. The aim of the present study was to evaluate the inhibitory effect of peracids with different length of hydrocarbon chain on the activity of selected PTPs. Methods: The enzymatic activity of human CD45, PTP1B, LAR, bacterial YopH was assayed under the cell-free conditions, and activity of cellular CD45 in human Jurkat cell lysates. The molecular docking and molecular dynamics were performed to evaluate the peracids binding to the CD45 active site. Results: Here we demonstrate that peracids reduce enzymatic activity of recombinant CD45, PTP1B, LAR, YopH and cellular CD45. Our studies indicate that peracids are more potent inhibitors of CD45 than hydrogen peroxide (with an IC50 value equal to 25 nM for peroctanoic acid and 8 µM for hydrogen peroxide). The experimental data show that the inactivation caused by peracids is dependent on hydrocarbon chain length of peracids with maximum inhibitory effect of medium-chain peracids (C8-C12 acyl chain), which correlates with calculated binding affinities to the CD45 active site. Conclusion: Peracids are potent inhibitors of PTPs with the strongest inhibitory effect observed for medium-chain peracids.

show abstract

“…This behavior has been investigated since peroxides play an important role in the modification of PP [33,34]. Klenk et al [35] reported that peroxides can be classified into seven different types depending on their reactivity based on their chemical structure, namely diacyl peroxides, peroxyesters, diperoxyketals, dialkyl peroxides, hydroperoxides, ketoneperoxides, and peroxydicarbonates. Additionally, Takamura et al [36] described the effectiveness of peroxides in cross-linking processes depending on their decomposition rates.…”

mentioning

confidence: 99%

Influence of Different Types of Peroxides on the Long-Chain Branching of PP via Reactive Extrusion

et al. 2020

View full text Add to dashboard Cite

Long-chain branching (LCB) is known as a suitable method to increase the melt strength behavior of linear polypropylene (PP), which is a fundamental weakness of this material. This enables the modification of various properties of PP, which can then be used—in the case of PP recyclates—as a practical “upcycling” method. In this study, the effect of five different peroxides and their effectiveness in building LCB as well as the obtained mechanical properties were studied. A single screw extruder at different temperatures (180 and 240 °C) was used, and long-chain branched polypropylene (PP-LCB) was prepared via reactive extrusion by directly mixing the peroxides. The peroxides used were dimyristyl peroxydicarbonate (PODIC C126), tert-butylperoxy isopropylcarbonate (BIC), tert-Butylperoxy 2-ethylhexyl carbonate (BEC), tert-amylperoxy 2-ethylhexylcarbonate (AEC), and dilauroyl peroxide (LP), all with a concentration of 20 mmol/kg. The influence of the temperature on the competitive prevalent reactions of degradation and branching was documented via melt mass-flow rate (MFR), rheology measurements, and gel permeation chromatography (GPC). However, via extensional rheology, strain hardening could be observed in all cases and the mechanical properties could be maintained or even improved. Particularly, PODIC C126 and LP signaled a promising possibility for LCB in this study.

show abstract

Peroxy Compounds, Organic

Abstract: The article contains sections titled: 1. Introduction 2. Alkyl Hydroperoxides … Show more

Cited by 27 publications

References 265 publications

KatG and KatE confer Acinetobacter resistance to hydrogen peroxide but sensitize bacteria to killing by phagocytic respiratory burst

KatG and KatE confer Acinetobacter resistance to hydrogen peroxide but sensitize bacteria to killing by phagocytic respiratory burst

Inactivation of Protein Tyrosine Phosphatases by Peracids Correlates with the Hydrocarbon Chain Length

Influence of Different Types of Peroxides on the Long-Chain Branching of PP via Reactive Extrusion

Contact Info

Product

Resources

About