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Journal ArticleDOI

The reactions of horseradish peroxidase, lactoperoxidase, and myeloperoxidase with enzymatically generated superoxide.

Diana Metodiewa, +1 more
- 01 Jul 1989 - 
- Vol. 272, Iss: 1, pp 245-253
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TLDR
It is tentatively concluded that in all cases compound III is formed in a two-step reaction of native enzyme with superoxide.
About
This article is published in Archives of Biochemistry and Biophysics.The article was published on 1989-07-01. It has received 43 citations till now. The article focuses on the topics: Lactoperoxidase & Horseradish peroxidase.

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Citations
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Journal ArticleDOI

Myeloperoxidase: friend and foe

TL;DR: It is concluded that the MPO system plays an important role in the microbicidal activity of phagocytes and the role of theMPO system in tissue injury.
Journal ArticleDOI

The role of O2.− in the production of HO.: in vitro and in vivo

TL;DR: In vivo O2 increases the supply of free iron by oxidatively attacking the [4Fe-4S] clusters of dehydratases such that they release Fe(II), which can then reduce H2O2.
Journal ArticleDOI

Extracellular superoxide dismutase in the airways of transgenic mice reduces inflammation and attenuates lung toxicity following hyperoxia

TL;DR: It is concluded that oxidative and inflammatory processes in the extracellular lung compartment contribute to hyperoxic-induced lung damage and that overexpression of hEC-SOD mediates a protective response to hyperoxia, at least in part, by attenuating the neutrophil inflammatory response.
Book ChapterDOI

Roles of Reactive Oxygen Species: Signaling and Regulation of Cellular Functions

TL;DR: Progress has been achieved in studying the oxidative activation of gene transcription in animal cells and bacteria and ROS are now considered signal molecules at nontoxic concentrations.
Journal ArticleDOI

Redox properties of the couples compound I/compound II and compound II/native enzyme of human myeloperoxidase.

TL;DR: Substantial differences between the two known heme peroxidase superfamilies are revealed and reflect the dramatic differences observed in the oxidisability of substrates by the MPO redox intermediates compound I and compound II.
References
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Journal ArticleDOI

Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase

TL;DR: It was shown that at any given pH and oxygen tension, the amount of univalently reduced oxygen, which was detectable in terms of the reduction of cytochrome c, rose as the turnover rate of the enzyme was decreased by decreasing the concentration of xanthine.
Journal ArticleDOI

Enthalpy of Decomposition of Hydrogen Peroxide by Catalase at 25C (with Molar Extinction Coefficients of H2O2 Solutions in the UV)

TL;DR: The enthalpy of decomposition of hydrogen peroxide by catalase has been determined calorimetrically in isotonic saline solutions at 25°C Extinction coefficients are also reported for hydrogen perox solutions in the ultraviolet as discussed by the authors.
Journal ArticleDOI

Mössbauer and electron paramagnetic resonance studies of horseradish peroxidase and its catalytic intermediates.

TL;DR: All evidence suggests a ferryl, OFeIV, state of the heme iron in compounds I and II and related complexes, and in the green compound I the iron weakly couples to a porphyrin radical with spin S' = 1/2.
Journal ArticleDOI

Protein control of prosthetic heme reactivity. Reaction of substrates with the heme edge of horseradish peroxidase.

TL;DR: The results imply that substrates interact with the heme edge rather than with the activated oxygen of Compounds I and II and specifically identify the region around the delta-meso-carbon and 8-methyl group as the exposed sector of theheme.
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