Stimulation of peroxidase reactions by hydroxamates.

@article{Brooks1983StimulationOP,
  title={Stimulation of peroxidase reactions by hydroxamates.},
  author={James L. Brooks},
  journal={Biochemical and biophysical research communications},
  year={1983},
  volume={116 3},
  pages={
          916-21
        }
}
  • J. L. Brooks
  • Published 15 November 1983
  • Chemistry, Medicine
  • Biochemical and biophysical research communications
Salicylhydroxamic acid, benzohydroxamic acid, and phenylacetohydroxamic acid were found to stimulate the oxidation of NADH, dithiothreitol, and ferrocyanide by horseradish peroxidase. The hydroxamates themselves served as substrates in peroxidase reactions, and the observed stimulations may involve hydroxamate free-radical formation. 
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The structure and functions of peroxidases are characterized. Attention is focused on the mechanisms of action of horseradish peroxidase in reactions with different substrates and on correlations
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Abstract Horseradish peroxidase or green algal cells catalyzed the NADH-dependent and oxygen-consuming oxidation of salicylhydroxamic acid (SHAM) to generate NO2−. NO2− production was inhibited by
Potent Reversible Inhibition of Myeloperoxidase by Aromatic Hydroxamates*
TLDR
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TLDR
It is concluded that despite a large capacity for peroxidase-mediated O 2 consumption, peroxIDase did not measurably contribute to control rates of O 2 Consumption in the absence of effectors.
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NAD(P)H oxidase and peroxidase activities in purified plasma membranes from cauliflower inflorescences.
Hydroxamate‐activated peroxidases in potato tuber callus. Interaction with the determination of the cytochrome and the alternative pathways
In potato (Solatium tuberosum L. cv. Bintje and Dore) callus a very active hydrox-amate-stimulated NADH-dependent O2-uptake develops during the growth of the callus, which is caused by a peroxidase.
Interactions between Cu(II), Mn(II) and salicylhydroxamic acid in determination of algal peroxidase activity
Abstract Cells of the green alga Selenastrum minutum have a high capacity for O 2 consumption mediated by extracellular peroxidase. The rate of peroxidase-mediated O 2 consumption is greatly
EXTRACELLULAR PEROXIDASE‐MEDIATED OXYGEN CONSUMPTION IN CHLAMYDOMONAS REINHARDTII (CHLOROPHYTA)1
TLDR
It is suggested that, despite a large capacity for peroxidase‐me‐diated O2 consumption, peroxidsase did not consume O2 at detectable rates in the absence of effectors, and measured rates of O1 consumption represented the rate of mitochondrial respiration.
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References

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The oxidation of dithiothreitol by peroxidases and oxygen.
TLDR
Evidence for horseradish peroxidase intermediates compound III and compound II has been observed, although ferroperoxid enzyme was not identified during the course of the reaction, although the stoichiometry has been extablished as 1 : 1 for oxygen consumed to dithiothreitol oxidized.
Oxidation of indole-3-acetic acid by peroxidase: involvement of reduced peroxidase and compound III with superoxide as a product.
TLDR
Kinetic and spectral data establish that peroxidase may oxidize indole-3-acetic acid by either of two pathways depending on the enzyme/substrate ratio, and important biological consequences may follow activation of this shuttle under physiological conditions.
Hydrogen Peroxide-mediated Oxidation of Indole-3-acetic Acid by Tomato Peroxidase and Molecular Oxygen.
TLDR
The stoichiometry of the reaction, which is highly dependent on enzyme concentration and pH, suggests that H( 2)O(2) initiates a sequence of reactions in which indole-3-acetic acid is oxidized.
Cell wall-bound malate dehydrogenase from horseradish
TLDR
In analogy to the known malate-oxalacetate shuttles, the possibility is discussed that this cell wall-associated malate dehydrogenase is involved in the transport of cytoplasmic reducing equivalents through the plasmalemma into the cell wall.
The oxidation of reduced pyridine nucleotides by peroxidase.
TLDR
Reduced pyridine nucleotides are oxidized aerobically in the presence of horse-radish peroxidase, Mn+2, and certain phenols, and a mechanism accounting for the oxidation of DPNH and TPNH is proposed.
Role of Peroxidase in Lignification of Tobacco Cells : II. Regulation by Phenolic Compounds.
TLDR
The results are discussed in relation to the role of cell wall peroxidases in conversion of coniferyl alcohol to lignin and in formation of H(2)O(2).
THE MECHANISM OF AEROBIC OXIDASE REACTION CATALYZED BY PEROXIDASE.
TLDR
It has been found that peroxidase catalyzes the formation of free radicals of hydrogen donors in the presence of H 2 O 2, and Compound III is not an active intermediate for dihydroxyfumarate oxidation.
Mechanism of thyroxine-mediated oxidation of reduced nicotinamide adenine dinucleotide in peroxidase-H2O2 system.
TLDR
The results suggest that the initial step of thyroxine-mediated NADH oxidation by HRP and H2O2 is the formation of oxidized thyroxines, a phenoxy radical, which attacks NADH to produce NAD.
Studies on horseradish peroxidase. X. The mechanism of the oxidation of p-cresol, ferrocyanide, and iodide by compound II.
Abstract Binding of p-crestol to native horseradish peroxidase was investigated by differential spectrophotometry, and the value 103 Kdiss = 3 m was obtained at neutral and acid pH; binding is not
Studies on Auxin Protectors: XI. Inhibition of Peroxidase-Catalyzed Oxidation of Glutathione by Auxin Protectors and o-Dihydroxyphenols.
TLDR
Commercial horseradish peroxidase, when supplemented with dichlorophenol and either manganese or hydrogen peroxide, will rapidly oxidize glutathione, but the addition of auxin protectors, or o-dihydroxyphenols, not only inhibited further oxidation of gluthathione but also caused a reappearance ofglutathione as if these antioxidants reduced a glutATHione oxidation intermediate.
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