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Home > Art, Film & Photography > EC 1.11: EC 1.11.1, Catalase, Peroxidase, Lactoperoxidase, Animal Heme-Dependent Peroxidases, Eosinophil Peroxidase, Glutathione Peroxidase
EC 1.11: EC 1.11.1, Catalase, Peroxidase, Lactoperoxidase, Animal Heme-Dependent Peroxidases, Eosinophil Peroxidase, Glutathione Peroxidase

EC 1.11: EC 1.11.1, Catalase, Peroxidase, Lactoperoxidase, Animal Heme-Dependent Peroxidases, Eosinophil Peroxidase, Glutathione Peroxidase


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About the Book

Purchase includes free access to book updates online and a free trial membership in the publisher's book club where you can select from more than a million books without charge. Chapters: Ec 1.11.1, Catalase, Peroxidase, Lactoperoxidase, Animal Heme-Dependent Peroxidases, Eosinophil Peroxidase, Glutathione Peroxidase, Peroxiredoxin, Myeloperoxidase, Horseradish Peroxidase, Thyroid Peroxidase, Haloperoxidase, Cytochrome C Peroxidase, Oxidative Enzyme. Excerpt: Catalase - Wikipedia, the free encyclopedia Catalase was first noticed as a substance in 1818 when Louis Jacques Thnard, who discovered H2O2 (hydrogen peroxide), suggested that its breakdown is caused by a substance. In 1900, Oscar Loew was the first to give it the name catalase, and found its presence in many plants and animals. In 1937 catalase from beef liver was crystallised by James B. Sumner and the molecular weight worked out in 1938. In 1969, the amino acid sequence of bovine catalase was worked out. Then in 1981, the 3D structure of the protein was revealed. The reaction of catalase in the decomposition of hydrogen peroxide is: 2 H2O2 2 H2O + O2 While the complete mechanism of catalase is not currently known, the reaction is believed to occur in two stages: H2O2 + Fe(III)-E H2O + O=Fe(IV)-E(.+)H2O2 + O=Fe(IV)-E(.+) H2O + Fe(III)-E + O2Here Fe()-E represents the iron centre of the heme group attached to the enzyme. Fe(IV)-E(.+) is a mesomeric form of Fe(V)-E, meaning that iron is not completely oxidized to +V but receives some "supporting electron" from the heme ligand. This heme has to be drawn then as radical cation (.+).As hydrogen peroxide enters the active site, it interacts with the amino acids Asn147 (asparagine at position 147) and His74, causing a proton (hydrogen ion) to transfer between the oxygen atoms. The free oxygen atom coordinates, freeing the newly-formed water molecule and Fe(IV)=O. Fe(IV)=O reacts with a second hydrogen peroxide molecule to re... More: http://booksllc.net/?id=37808


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Product Details
  • ISBN-13: 9781157819950
  • Publisher: Books LLC
  • Publisher Imprint: Books LLC
  • Height: 152 mm
  • No of Pages: 64
  • Spine Width: 4 mm
  • Weight: 104 gr
  • ISBN-10: 1157819958
  • Publisher Date: 09 Jun 2010
  • Binding: Paperback
  • Language: English
  • Returnable: N
  • Sub Title: EC 1.11.1, Catalase, Peroxidase, Lactoperoxidase, Animal Heme-Dependent Peroxidases, Eosinophil Peroxidase, Glutathione Peroxidase
  • Width: 229 mm


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