Publication Cover
Redox Report
Communications in Free Radical Research
Volume 5, 2000 - Issue 4
376
Views
39
CrossRef citations to date
0
Altmetric
Miscellany

The reactivity of myeloperoxidase compound I formed with hypochlorous acid

, , , &
Pages 173-178 | Published online: 19 Jul 2013

  • Kimura S, Ikeda-Saito M. Human myeloperoxidase and thyroid peroxidase, two enzymes with separate and distinct physiological functions, are evolutionarily related members of the same gene family. Proteins Struct Funct Genet 1988; 3: 113–120.
  • Sakamaki K, Tomonaga M, Tsukui K, Nagata S. Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J Biol Chem 1989; 264: 16828–16836.
  • Cals MM, Mailliart P, Brignon G, Anglade P, Dumas BR. Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. Eur J Biochem 1991; 198: 733–739.
  • Harrison JE, Schultz J. Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 1976; 251: 1371–1376.
  • Fiedler TJ, Davey CA, Feima RE. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8 A resolution. J Biol Chem 2000; 275: 11964–11971.
  • Marquez L, Huang JT, Dunford FIB. Spectral and kinetic studies on the formation of myeloperoxidase compounds I and II: roles of hydrogen peroxide and superoxide. Biochemistry 1994; 33: 1447–1454.
  • Bolscher BGJM, Weyer R. A kinetic study of the reaction between human myloperoxidase, hydroperoxides and cyanide. Inhibition by chloride and thiocyanate. Biochim Biophys Acta 1984; 788: 1–10.
  • Iwamoto H, Kobayashi T, Hasegawa E, Morita Y. Reaction of human myeloperoxidase with hydrogen peroxide and its true catalase activity. J Biochem 1987; 101: 1407–1412.
  • Lardinois OM, Ortiz de Montenano PR. EPR spin-trapping of a myeloperoxidase protein radical. Biochem Biophys Res Commit 2000; 270: 199–202.
  • Floris R, Weyer R. Reaction of myeloperoxidase with its product HOC1. Eur J Biochem 1992; 207: 697–702.
  • Furtmüller PG, Burner U, Obinger C. Reaction of myeloperoxidase compound I with chloride, bromide, iodide and thiocyanate. Biochemistry 1998; 37: 17923–17930.
  • Burner U, Furtmiiller PG, Kettle AJ, Koppenol WH, Obinger C. Mechanism of reaction of myeloperoxidase with nitrite. J Biol Chem 2000; 275: 20597–20601.
  • Morris C. The acid ionization constant of HOC1 from 5° to 350. J Phys Chem 1966; 70: 3798–3805.
  • Ikeda-Saito M. Spectroscopic, ligand binding, and enzymatic properties of the spleen green hemoprotein. J Biol Chem 1985; 260: 11688–11696.
  • Riddles PW, Blakely RL, Zerner B. Reassessment of Ellman's reagent. Methods Enzymol 1983; 91: 49–60.
  • Marquez LA, Dunford FIB. Kinetics of oxidation of tyrosine and dityrosine by myeloperoxidase compounds I and II. J Biol Chem 1995; 270: 30434–30440.
  • Hsuanyu Y, Dunford FIB. Oxidation of clozapine and ascorbate by myeloperoxidase. Arch Biochem Biophys 1999; 368: 413–420.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.