Myeloperoxidase and singlet oxygen: a reappraisal

Harrison, John; Watson, Brant D.; Schultz, Julius

doi:10.1016/0014-5793(78)80780-7

Cited by 72 publications

(45 citation statements)

References 10 publications

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“…Despite numerous studies, the formation of OH°i n phagocytes is still controversial (Britigan et al, 1986;Rosen and Klebanoff, 1979;Tauber and Babior, 1977;Ward et al, 1983). The formation of singlet oxygen appears to be an important event in the microbicidal potential of neutrophils (Allen et al, 1972;Harrison et al, 1978).…”

Section: Nadph-derived Oxidantsmentioning

confidence: 99%

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Witko‐Sarsat

Rieu

Descamps‐Latscha

et al. 2000

Laboratory Investigation

952

723

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Section: Nadph-derived Oxidantsmentioning

confidence: 99%

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Witko‐Sarsat

Rieu

Descamps‐Latscha

et al. 2000

Laboratory Investigation

952

723

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“…1) catalyzed by myeloperoxidase (MPO) (1)(2)(3)(4). This heme enzyme is stored at high concentrations in the granules of phagocytic cells (neutrophils and monocytes), and, upon stimulation, it is secreted into both the extracellular milieu and the phagocytic vacuole (3).…”

mentioning

confidence: 99%

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

Miyamoto

Martinez²,

Rettori³

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

124

108

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The reaction of hypochlorous acid (HOCl) with hydrogen peroxide is known to generate stoichiometric amounts of singlet molecular oxygen [O2 ( 1 ⌬g)]. This study shows that HOCl can also react with linoleic acid hydroperoxide (LAOOH), generating O2 ( 1 ⌬g) with a yield of 13 ؎ 2% at physiological pH. Characteristic light emission at 1,270 nm, corresponding to O2 ( 1 ⌬g) monomolecular decay, was observed when HOCl was reacted with LAOOH or with liposomes containing phosphatidylcholine hydroperoxides, but not with cumene hydroperoxide or tert-butyl hydroperoxide. The generation of O2 ( 1 ⌬g lipid hydroperoxides ͉ mass spectrometry ͉ myeloperoxidase ͉ near-infrared emission ͉ 18 O-labeled oxygen

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“…This suggests that diazobicyclooctane and histidine also react with hypochlorite. Furthermore, bromine or chlorine water has been found to react with diphenylfuran, methionine, histidine and diazobicyclooctane [43]. Thus the diphenylfuran oxidation observed in this paper could be due to hypobromite or bromine formed from the hypobromite.…”

mentioning

confidence: 56%

Singlet Oxygen Formation by a Peroxidase, H₂O₂ and Halide System

Piatt

O’Brien

1979

European Journal of Biochemistry

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Evidence for singlet oxygen formation has been obtained for the lactoperoxidase, H 2 0 2 and bromide system by monitoring 2,3-diphenyIfuran and diphenylisobenzofuran oxidation, 0 2 evolution, and chemiluminescence. This could provide an explanation for the cytotoxic and microbicidal activity of peroxidases and polymorphonuclear leukocytes. Evidence for singlet oxygen formation included the following. (a) Chemiluminescence accompanying the enzymic reaction was doubled in a deuterated buffer and inhibited by singlet oxygen traps. (b) The singlet oxygen traps, diphenylfuran and diphenylisobenzofuran, were oxidized to their known singlet oxygen oxidation products in the presence of lactoperoxidase, hydrogen peroxide and bromide. (c) The rate of oxidation of diphenylfuran and diphenylisobenzofuran was inhibited when monitored in the presence of known singlet oxygen traps or quenchers. (d) Oxygen evolution from the enzymic reaction was inhibited by singlet oxygen traps but not by singlet oxygen quenchers. (e) The traps or quenchers which were effective inhibitors in the experiments above did not inhibit peroxidase activity, were not competitive peroxidase substrates and did not react with the hypobromite intermediate since they did not inhibit hydrogen peroxide consumption by the enzyme.Using these criteria, various biological molecules were tested for their reactivity with singlet oxygen. Furthermore, by studying their effect on oxygen release by the enzymic reaction, it could be ascertained whether they were acting as singlet oxygen traps or quenchers.The microbicidal activity of myeloperoxidase or lactoperoxidase, hydrogen peroxide, and halides has been described by Klebanoff [I -31. These peroxidase systems have aIso been shown to be cytotoxic to tumor cells [4,5] as well as a variety of bacterial, fungal and viral species. The nature of the toxic component of these systems has not been determined but mounting evidence points to singlet oxygen ('02*) involvement. The microbicidal [6] and cytotoxic [7] property of chemically generated ' 0 2 * has been established. Krinsky has found that a carotenoidless mutant organism was killed rapidly by polymorphonuclear leukocytes, unlike the wild-type strain containing the '02* quencing carotenoids [S]. Direct evidence for '02* involvement has come from experiments by Allen and coworkers where it was shown that phagocytizing polymorphonuclear leukocytes [9] and isolated myeloperoxidase [ l o ] in the presence of H202 and C1-, emitted light which could be due to the relaxation of excited singlet oxygen to its ground state (triplet oxygen). Klebanoff has been able to inhibit the micro-____ bicidal activity of phagocytizing polymorphonuclear leukocytes using a '02* trap [6]. In a preliminary communication we have also demonstrated that the lactoperoxidase system can convert 2,5-diphenylfuran to its specific singlet oxygen product, cis-dibenzoyl ethylene [I I].Inhibition of this conversion using ' 0 2 * quenchers, and stimulation of conversion in 'H20 buffer (in which the half-l...

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Myeloperoxidase and singlet oxygen: a reappraisal

Cited by 72 publications

References 10 publications

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

Singlet Oxygen Formation by a Peroxidase, H₂O₂ and Halide System

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Myeloperoxidase and singlet oxygen: a reappraisal

Cited by 72 publications

References 10 publications

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Neutrophils: Molecules, Functions and Pathophysiological Aspects

Linoleic acid hydroperoxide reacts with hypochlorous acid, generating peroxyl radical intermediates and singlet molecular oxygen

Singlet Oxygen Formation by a Peroxidase, H2O2 and Halide System

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Singlet Oxygen Formation by a Peroxidase, H₂O₂ and Halide System