ArticleThe Biochemical journal1995
Thiocyanate, a plausible physiological electron donor of gastric peroxidase.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 50 citations in OpenAlex.
- Lactoperoxidase: Properties, Functions, and Potential Applications.International journal of molecular sciences · 2025Review
- Hypothiocyanite and host-microbe interactions.Molecular microbiology · 2023Article
- Structural evidence of the oxidation of iodide ion into hyper-reactive hypoiodite ion by mammalian heme lactoperoxidase.Protein science : a publication of the Protein Society · 2022Article
- The Role of Thiocyanate in Modulating Myeloperoxidase Activity during Disease.International journal of molecular sciences · 2020Review
- Clinical, clinicopathologic, and gastrointestinal changes from administration of clopidogrel, prednisone, or combination in healthy dogs: A double-blind randomized trial.Journal of veterinary internal medicine · 2019Article
- Clinical, clinicopathologic, and gastrointestinal changes from aspirin, prednisone, or combination treatment in healthy research dogs: A double-blind randomized trial.Journal of veterinary internal medicine · 2019Article
- Susceptibility of influenza viruses to hypothiocyanite and hypoiodite produced by lactoperoxidase in a cell-free system.PloS one · 2018Article
- Pseudomonas aeruginosa defense systems against microbicidal oxidants.Molecular microbiology · 2017Article
- Hashimoto's Thyroiditis and Autoimmune Gastritis.Frontiers in endocrinology · 2017Review
- Biochemical mechanisms and therapeutic potential of pseudohalide thiocyanate in human health.Free radical research · 2015Review
- Selective metabolism of hypothiocyanous acid by mammalian thioredoxin reductase promotes lung innate immunity and antioxidant defense.The Journal of biological chemistry · 2013Article
- Thiocyanate: a potentially useful therapeutic agent with host defense and antioxidant properties.Biochemical pharmacology · 2012Article
- The myeloperoxidase-derived oxidant HOSCN inhibits protein tyrosine phosphatases and modulates cell signalling via the mitogen-activated protein kinase (MAPK) pathway in macrophages.The Biochemical journal · 2010Article
- Pro-inflammatory activity in rats of thiocyanate, a metabolite of the hydrocyanic acid inhaled from tobacco smoke.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2009Article
- Effects of ascorbic acid, glutathione, thiocyanate, and iodide on antimicrobial activity of acidified nitrite.Antimicrobial agents and chemotherapy · 2004Article
- Probing the role of active site histidine residues in the catalytic activity of lacrimal gland peroxidase.Molecular and cellular biochemistry · 2002Article
- Dexamethasone makes the gastric mucosa susceptible to ulceration by inhibiting prostaglandin synthetase and peroxidase--two important gastroprotective enzymes.Molecular and cellular biochemistry · 1999Article
- Characterization of sheep lacrimal-gland peroxidase and its major physiological electron donor.The Biochemical journal · 1996Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gastric peroxidase (GPO) was purified to apparent homogeneity to characterize its major physiological electron donor. The enzyme (RZ = 0.7), with a subunit molecular mass of 50 kDa, is a glycoprotein, with a relative abundance of aspartic and glutamic acid over arginine and lysine. It has a Soret maximum at 412 nm, which is shifted to 426 nm by H2O2 due to formation of compound II. Although the physiological electron donors I-, Br- and SCN-, but not Cl-, are oxidized by GPO optimally at acid pH, only I- and SCN- are oxidized appreciably at physiological pH. Considering that the I- concentration in stomach is less than 1 microM, whereas the SCN- concentration is about 250 microM, SCN- may act as a major electron donor for GPO. Moreover, SCN- oxidation remains unaltered in the presence of physiological concentrations of other halides. The second-order rate constant for the reaction of GPO with H2O2 (k1) and compound I with SCN- (k2) at pH 7 was found to be 8 x 10(7) M-1.s-1 and 2 x 10(5) M-1.s-1 respectively. GPO has significant pseudocatalase activity also in the presence of I- or Br-, but it is blocked by SCN-. The SCN- oxidation product OSCN- may be reduced back to SCN- by cellular GSH, and GSSG may be reduced back to GSH by glutathione reductase and NADPH. In a system reconstituted with pure glutathione reductase, NADPH, GSH, SCN- and H2O2. GPO-catalysed SCN- oxidation could be coupled to NADPH oxidation. This system where GPO utilizes SCN- as the major physiological electron donor may operate efficiently to scavenge intracellular H2O2.
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