{"product_id":"peroxidases-and-catalases-9780470224762","title":"Peroxidases and Catalases","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003cb\u003eSINGLE SOURCE GUIDE TO PEROXIDASES AND CATALASES\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eReflecting the important historical discoveries and exciting research in the field in recent years, \u003ci\u003ePeroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology\u003c\/i\u003e provides a much-needed systematic, up-to-date treatment of peroxidases and catalases.\u003c\/p\u003e \u003cp\u003eFrom the structure and properties of the various superfamilies to current applications of peroxidases, the book consolidates vast amounts of information previously scattered in the professional literature, covering all aspects of these ubiquitous enzymes that act on a variety of substances and processes in living systemstheir properties, reactions, crystal structures, cloning, and more.\u003c\/p\u003e \u003cp\u003eConsidering the subject from both theoretical and applied perspectives, \u003ci\u003ePeroxidases and Catalases\u003c\/i\u003e offers a critical review of the literature and detailed discussions of the most current research. Chapters cover:\u003c\/p\u003e \u003cul\u003e \u003cli\u003eThe background and hist\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003cp\u003ePreface xiii\u003c\/p\u003e \u003cp\u003eContributors xv\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Historical: Pioneering Work on Horseradish and Yeast Cytochrome\u003ci\u003e c\u003c\/i\u003e Peroxidases 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 1\u003c\/p\u003e \u003cp\u003eTechniques and Instrumentation 2\u003c\/p\u003e \u003cp\u003eSummary and Conclusions 5\u003c\/p\u003e \u003cp\u003eReferences 6\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Heme Peroxidase and Catalase Families 9\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003ePlant, Fungal, and Bacterial Peroxidases 9\u003c\/p\u003e \u003cp\u003eMammalian Peroxidases 11\u003c\/p\u003e \u003cp\u003eCatalases 12\u003c\/p\u003e \u003cp\u003eReferences 12\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Horseradish Peroxidase. I. The Native Enzyme, Compounds I and II, Their Structures, and Their Cycle 13\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 13\u003c\/p\u003e \u003cp\u003eThe Classic Peroxidase Cycle 13\u003c\/p\u003e \u003cp\u003eStructure and Properties of Native Horseradish Peroxidase C 18\u003c\/p\u003e \u003cp\u003eHorseradish Peroxidase Compound I (HRP-I) 23\u003c\/p\u003e \u003cp\u003eHorseradish Peroxidase Compound II (HRP-II) 26\u003c\/p\u003e \u003cp\u003eSome Diverse Approaches to an Understanding of Horseradish Peroxidase 27\u003c\/p\u003e \u003cp\u003eReferences 30\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Horseradish Peroxidase. II. Two-Electron Reactions, Ferrous Peroxidase, Compound III, The Five Oxidation States, Oxygen Evolution, and Inactivation 41\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 41\u003c\/p\u003e \u003cp\u003eTwo-Electron Oxidations By Compound I 41\u003c\/p\u003e \u003cp\u003eOxygen Transfer By One-Electron Mechanisms 44\u003c\/p\u003e \u003cp\u003eFerrous Horseradish Peroxidase and Compound III 45\u003c\/p\u003e \u003cp\u003eThe Five Oxidation States of Horseradish Peroxidase 48\u003c\/p\u003e \u003cp\u003eThe Catalatic Reaction 50\u003c\/p\u003e \u003cp\u003eThe HRP Clock Reaction 51\u003c\/p\u003e \u003cp\u003eEnzyme Inactivation 51\u003c\/p\u003e \u003cp\u003eReferences 52\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Horseradish Peroxidase. III. Oscillations and Peroxidase-Oxidase Reactions with NADH, Indole-3- Acetic Acid, and Isobutyraldehyde. Light Emission 57\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eOscillations and the NADH Peroxidase-Oxidase Reaction 57\u003c\/p\u003e \u003cp\u003ePeroxidase Oxidase Reaction with Indole-3-Acetic Acid 63\u003c\/p\u003e \u003cp\u003eReaction of Isobutyraldehyde with Horseradish Peroxidase 68\u003c\/p\u003e \u003cp\u003eReferences 70\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Yeast Cytochrome \u003ci\u003ec\u003c\/i\u003e Peroxidase: Reactions with Small Substrates 77\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 77\u003c\/p\u003e \u003cp\u003eProperties of Yeast Cytochrome\u003ci\u003e c\u003c\/i\u003e Peroxidase 77\u003c\/p\u003e \u003cp\u003eCrystal Structures of Yeast Cytochrome\u003ci\u003e c\u003c\/i\u003e Peroxidase, its Compounds and Complexes 78\u003c\/p\u003e \u003cp\u003eMechanism of Compound I Formation 80\u003c\/p\u003e \u003cp\u003eThe Reaction Cycle for Yeast Cytochrome \u003ci\u003ec\u003c\/i\u003e Peroxidase 82\u003c\/p\u003e \u003cp\u003eSteady-State Kinetics 83\u003c\/p\u003e \u003cp\u003eReferences 91\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Yeast Cytochrome\u003ci\u003e c\u003c\/i\u003e Peroxidase: Reaction with Cytochrome \u003ci\u003ec\u003c\/i\u003e 97\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 97\u003c\/p\u003e \u003cp\u003eExperimental Results 97\u003c\/p\u003e \u003cp\u003eReferences 103\u003c\/p\u003e \u003cp\u003e\u003cb\u003e8 Spectroscopy. I. Optical, Resonance Raman, and X-Ray Absorption 107\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eOptical Absorption Spectra 107\u003c\/p\u003e \u003cp\u003eResonance Raman Spectra 111\u003c\/p\u003e \u003cp\u003eX-ray Absorption Spectroscopy 121\u003c\/p\u003e \u003cp\u003eReferences 123\u003c\/p\u003e \u003cp\u003e\u003cb\u003e9 Spectroscopy. II. Nuclear Magnetic Resonance, Electron Spin, and M\u003c\/b\u003e\u003cb\u003eöSsbauer 129\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eNuclear Magnetic Resonance (NMR) Spectroscopy 129\u003c\/p\u003e \u003cp\u003eElectron Spin Resonance (ESR) Spectroscopy 139\u003c\/p\u003e \u003cp\u003eMössbauer Spectroscopy 145\u003c\/p\u003e \u003cp\u003eReferences 146\u003c\/p\u003e \u003cp\u003e\u003cb\u003e10 Theoretical 153\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003ePeroxidase Kinetics 153\u003c\/p\u003e \u003cp\u003eMarcus Theory for Electron Transfer Reactions 156\u003c\/p\u003e \u003cp\u003eElectron Tunneling 159\u003c\/p\u003e \u003cp\u003eElectron Transfer Reactions in Proteins 160\u003c\/p\u003e \u003cp\u003eElectron Density Circuits 161\u003c\/p\u003e \u003cp\u003eDiffusion Control 163\u003c\/p\u003e \u003cp\u003eQuantum Mechanical Calculations 164\u003c\/p\u003e \u003cp\u003eReferences 171\u003c\/p\u003e \u003cp\u003e\u003cb\u003e11 Class I: Ascorbate Peroxidase 179\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 179\u003c\/p\u003e \u003cp\u003eSequencing and Cloning 180\u003c\/p\u003e \u003cp\u003eProperties, Reactions, and Intermediate Compounds 181\u003c\/p\u003e \u003cp\u003eCrystal Structures 184\u003c\/p\u003e \u003cp\u003eReferences 185\u003c\/p\u003e \u003cp\u003e\u003cb\u003e12 Catalase-Peroxidases and Mycobacterium Tuberculosis 189\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 189\u003c\/p\u003e \u003cp\u003eStructures of Catalase-Peroxidases 190\u003c\/p\u003e \u003cp\u003eIsoniazid and Other Reactants of Catalase-Peroxidases 192\u003c\/p\u003e \u003cp\u003eThe Oxidative Defense Mechanisms of Mycobacterium Tuberculosis 196\u003c\/p\u003e \u003cp\u003eReferences 196\u003c\/p\u003e \u003cp\u003e\u003cb\u003e13 Class II. Lignin, Manganese, Versatile, and Coprinus Cinereus Peroxidases 203\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eLignin Peroxidase 203\u003c\/p\u003e \u003cp\u003eManganese Peroxidase 208\u003c\/p\u003e \u003cp\u003eOther Manganese Peroxidases, Versatile Peroxidase 210\u003c\/p\u003e \u003cp\u003eCoprinus Cinereus (Arthromyces Ramosus) Peroxidase 210\u003c\/p\u003e \u003cp\u003eReferences 212\u003c\/p\u003e \u003cp\u003e\u003cb\u003e14 Other Class III Peroxidases 221\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eArabidopsis Thaliana Peroxidase 221\u003c\/p\u003e \u003cp\u003eBarley Peroxidase 222\u003c\/p\u003e \u003cp\u003ePeanut Peroxidase 223\u003c\/p\u003e \u003cp\u003eSoybean Peroxidase 225\u003c\/p\u003e \u003cp\u003eTobacco Peroxidases 225\u003c\/p\u003e \u003cp\u003eTurnip Peroxidases 226\u003c\/p\u003e \u003cp\u003eReferences 227\u003c\/p\u003e \u003cp\u003e\u003cb\u003e15 Catalases 233\u003cbr\u003e\u003c\/b\u003e\u003ci\u003ePeter Jones\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 233\u003c\/p\u003e \u003cp\u003ePerspective 234\u003c\/p\u003e \u003cp\u003eProgress 235\u003c\/p\u003e \u003cp\u003eCatalases in Biology 248\u003c\/p\u003e \u003cp\u003eProspects 250\u003c\/p\u003e \u003cp\u003eReferences 252\u003c\/p\u003e \u003cp\u003e\u003cb\u003e16 Myeloperoxidase: Enzymology 257\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 257\u003c\/p\u003e \u003cp\u003eProperties of Myeloperoxidase 258\u003c\/p\u003e \u003cp\u003eThe Compounds of Myeloperoxidase 260\u003c\/p\u003e \u003cp\u003eReactions of Myeloperoxidase 264\u003c\/p\u003e \u003cp\u003eCloning of Myeloperoxidase: Site-Directed Mutagenesis 266\u003c\/p\u003e \u003cp\u003eThe Crystal Structure and the Prosthetic Group of Myeloperoxidase 266\u003c\/p\u003e \u003cp\u003eEosinophil Peroxidase 268\u003c\/p\u003e \u003cp\u003eReferences 269\u003c\/p\u003e \u003cp\u003e\u003cb\u003e17 Biomedical Aspects of Myeloperoxidase: Halogenation Reactions In Cardiovascular Disease, Infection, And Cancer 281\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eJeffrey P. Henderson and Jay. W. Heinecke\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 281\u003c\/p\u003e \u003cp\u003eOxidants Produced by MPO in Humans 281\u003c\/p\u003e \u003cp\u003eMPO and Coronary Artery Disease 286\u003c\/p\u003e \u003cp\u003eMPO and Carcinogenesis 288\u003c\/p\u003e \u003cp\u003eProspects 290\u003c\/p\u003e \u003cp\u003eReferences 290\u003c\/p\u003e \u003cp\u003e\u003cb\u003e18 Prostaglandin H Synthase 297\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 297\u003c\/p\u003e \u003cp\u003eCrystal Structures 299\u003c\/p\u003e \u003cp\u003eProstaglandin H Synthase-2 300\u003c\/p\u003e \u003cp\u003ePreliminary Mechanistic Studies 302\u003c\/p\u003e \u003cp\u003eDetection of Free Radicals: Role of ESR Spectroscopy 303\u003c\/p\u003e \u003cp\u003eThe Role of Aspirin and Related Substances: Contributions of Vane and Smith 304\u003c\/p\u003e \u003cp\u003eWork of Marnett and Coworkers 305\u003c\/p\u003e \u003cp\u003eWork of Kulmacz, Tsai, and Coworkers 305\u003c\/p\u003e \u003cp\u003eManganese Prostaglandin Synthases 306\u003c\/p\u003e \u003cp\u003eMechanistic Details 307\u003c\/p\u003e \u003cp\u003eReferences 314\u003c\/p\u003e \u003cp\u003e\u003cb\u003e19 Thyroid Peroxidase 323\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 323\u003c\/p\u003e \u003cp\u003eHormone Discovery and Chemical Synthesis 324\u003c\/p\u003e \u003cp\u003eDetection of the Method of Biological Synthesis of Thyroxine 325\u003c\/p\u003e \u003cp\u003eConclusions 329\u003c\/p\u003e \u003cp\u003eReferences 329\u003c\/p\u003e \u003cp\u003e\u003cb\u003e20 Lacto- And Salivary Peroxidases 335\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 335\u003c\/p\u003e \u003cp\u003eProperties 335\u003c\/p\u003e \u003cp\u003eThe Compounds of Lactoperoxidase and Their Reactions 336\u003c\/p\u003e \u003cp\u003eReferences 339\u003c\/p\u003e \u003cp\u003e\u003cb\u003e21 Chloroperoxidase From\u003ci\u003e C. Fumago \u003c\/i\u003e345\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 345\u003c\/p\u003e \u003cp\u003eHistory 345\u003c\/p\u003e \u003cp\u003eOptical Spectra 347\u003c\/p\u003e \u003cp\u003eESR, Endor, Mössbauer, Exafs, and Resonance Raman Spectra 348\u003c\/p\u003e \u003cp\u003eInvestigations of Compounds I and II 348\u003c\/p\u003e \u003cp\u003eStructure of Compound I and the Catalatic Reaction 349\u003c\/p\u003e \u003cp\u003eLigand Binding 350\u003c\/p\u003e \u003cp\u003eKinetics and Mechanisms of Chlorination and Oxidation 351\u003c\/p\u003e \u003cp\u003eAmino Acid Sequence and Crystal Structure 353\u003c\/p\u003e \u003cp\u003eReferences 353\u003c\/p\u003e \u003cp\u003e\u003cb\u003e22 Selenium-Containing Enzymes: Glutathione Peroxidase and Iodothyronine Deiodinase 359\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 359\u003c\/p\u003e \u003cp\u003eGlutathione Peroxidase 359\u003c\/p\u003e \u003cp\u003eIodothyronine Deiodinase 361\u003c\/p\u003e \u003cp\u003eReferences 361\u003c\/p\u003e \u003cp\u003e\u003cb\u003e23 Structure and Function of Vanadium Haloperoxidases 363\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRon Wever and Rokus Renirie\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eSummary 363\u003c\/p\u003e \u003cp\u003eAbbreviations 364\u003c\/p\u003e \u003cp\u003eIntroduction 364\u003c\/p\u003e \u003cp\u003eOccurrence and Biological Function of Vanadium Iodo- and Bromoperoxidases 365\u003c\/p\u003e \u003cp\u003eOccurrence and Biological Function of Vanadium Chloroperoxidases 366\u003c\/p\u003e \u003cp\u003eCatalytic Properties of Bromoperoxidase 367\u003c\/p\u003e \u003cp\u003eProperties of the Prosthetic Group in Bromoperoxidase 370\u003c\/p\u003e \u003cp\u003eKinetic and Optical Properties of Vanadium Chloroperoxidases 371\u003c\/p\u003e \u003cp\u003eSulfoxidation Reactions 373\u003c\/p\u003e \u003cp\u003eStability of Bromo- and Chloroperoxidases 374\u003c\/p\u003e \u003cp\u003eX-ray Structures of Vanadium Bromoperoxidases 374\u003c\/p\u003e \u003cp\u003eActive Site of Vanadium Bromoperoxidase From \u003ci\u003eA. Nodosum\u003c\/i\u003e 375\u003c\/p\u003e \u003cp\u003eX-ray Structures of the Vanadium Chloroperoxidase and Details of the Active Site 376\u003c\/p\u003e \u003cp\u003eX-ray Structure of the Peroxo-Intermediate of Vanadium Chloroperoxidase and Difference in Reactivity Between Chloro- and Bromoperoxidases 378\u003c\/p\u003e \u003cp\u003eNature of the Vanadate Cofactor 380\u003c\/p\u003e \u003cp\u003eReferences 382\u003c\/p\u003e \u003cp\u003e\u003cb\u003e24 Other Heme Peroxidases and Enzymes 387\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eDI-Heme Peroxidases 387\u003c\/p\u003e \u003cp\u003ePeroxidases Everywhere You Look 389\u003c\/p\u003e \u003cp\u003eMyoglobins 391\u003c\/p\u003e \u003cp\u003eHemoglobin 392\u003c\/p\u003e \u003cp\u003eCytochrome\u003ci\u003e c\u003c\/i\u003e Oxidase 392\u003c\/p\u003e \u003cp\u003eOxygenases 392\u003c\/p\u003e \u003cp\u003eHeme Oxygenase 394\u003c\/p\u003e \u003cp\u003eGuanylyl Cyclase 394\u003c\/p\u003e \u003cp\u003eReferences 395\u003c\/p\u003e \u003cp\u003e\u003cb\u003e25 Application of Peroxidases 403\u003cbr\u003e \u003c\/b\u003e\u003ci\u003eRon Wever\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIntroduction 403\u003c\/p\u003e \u003cp\u003eBackground Information 403\u003c\/p\u003e \u003cp\u003ePeroxidases as Pharmaceutical and\/or Antimicrobial Agents 404\u003c\/p\u003e \u003cp\u003eApplications in Bleaching and Detergents 411\u003c\/p\u003e \u003cp\u003eBiotransformations 412\u003c\/p\u003e \u003cp\u003ePolymerization Reactions and Wastewater Purification 414\u003c\/p\u003e \u003cp\u003eDepolymerization Reactions 415\u003c\/p\u003e \u003cp\u003eAnalytical Applications 416\u003c\/p\u003e \u003cp\u003eMedical Applications 417\u003c\/p\u003e \u003cp\u003eReferences 417\u003c\/p\u003e \u003cp\u003eAuthor Index 425\u003c\/p\u003e \u003cp\u003eSubject Index 451\u003c\/p\u003e\n\u003c\/li\u003e\n\u003c\/ul\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":53515415781719,"sku":"9780470224762","price":184.46,"currency_code":"GBP","in_stock":true}],"url":"https:\/\/bookcurl.com\/products\/peroxidases-and-catalases-9780470224762","provider":"Book Curl","version":"1.0","type":"link"}