{"product_id":"chemistry-of-metalloproteins-9781118470442","title":"Chemistry of Metalloproteins","description":"\u003cb\u003eBook Synopsis\u003c\/b\u003e\u003cbr\u003e\u003cp\u003e\u003cb\u003eAddresses the full gamut of questions in metalloprotein science\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eFormatted as a question-and-answer guide, this book examines all major families of metal binding proteins, presenting our most current understanding of their structural, physicochemical, and functional properties. Moreover, it introduces new and emerging medical applications of metalloproteins. Readers will discover both the underlying chemistry and biology of this important area of research in bioinorganic chemistry.\u003c\/p\u003e \u003cp\u003e\u003ci\u003eChemistry of Metalloproteins\u003c\/i\u003e features a building block approach that enables readers to master the basics and then advance to more sophisticated topics. The book begins with a general introduction to bioinorganic chemistry and metalloproteins. Next, it covers:\u003c\/p\u003e \u003cul\u003e \u003cli\u003eAlkali and alkaline earth cations\u003c\/li\u003e \u003cli\u003eMetalloenzymes\u003c\/li\u003e \u003cli\u003eCopper proteins\u003c\/li\u003e \u003cli\u003eIron proteins\u003c\/li\u003e \u003cli\u003eVitamin B\u003csub\u003e12\u003c\/sub\u003e\n\u003c\/li\u003e \u003cli\u003eChlorophyll\u003c\/li\u003e \u003c\/ul\u003e \u003cp\u003eChapters are richly illustrated to h\u003cbr\u003e\u003cbr\u003e\u003cb\u003eTable of Contents\u003c\/b\u003e\u003cbr\u003e\u003c\/p\u003e\u003cp\u003ePreface ix\u003c\/p\u003e \u003cp\u003e\u003cb\u003e1 Introduction 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eProteins: Formation, Structures, and Metalloproteins, 4\u003c\/p\u003e \u003cp\u003eReferences, 28\u003c\/p\u003e \u003cp\u003e\u003cb\u003e2 Alkali and Alkaline Earth Cations 31\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eReferences, 67\u003c\/p\u003e \u003cp\u003e\u003cb\u003e3 Nonredox Metalloenzymes 71\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eCarboxypeptidases, 75\u003c\/p\u003e \u003cp\u003eCarbonic Anhydrase, 84\u003c\/p\u003e \u003cp\u003eAlcohol Dehydrogenase, 88\u003c\/p\u003e \u003cp\u003eReferences, 91\u003c\/p\u003e \u003cp\u003e\u003cb\u003e4 Copper Proteins 95\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction, 95\u003c\/p\u003e \u003cp\u003eElectronic Spectra of Copper Ions, 96\u003c\/p\u003e \u003cp\u003eESR Spectra of Copper Ions, 105\u003c\/p\u003e \u003cp\u003eCopper Proteins, 117\u003c\/p\u003e \u003cp\u003ePlastocyanin, 119\u003c\/p\u003e \u003cp\u003eAzurin and Stellacyanin, 127\u003c\/p\u003e \u003cp\u003eSuperoxide Dismutase, 131\u003c\/p\u003e \u003cp\u003eHemocyanin, 135\u003c\/p\u003e \u003cp\u003eAscorbic Oxidase, 139\u003c\/p\u003e \u003cp\u003eReferences, 142\u003c\/p\u003e \u003cp\u003e\u003cb\u003e5 Iron Proteins 147\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eIntroduction, 147\u003c\/p\u003e \u003cp\u003eElectronic Spectra of Iron Ions, 148\u003c\/p\u003e \u003cp\u003eMössbauer Spectroscopy of Iron Ions, 155\u003c\/p\u003e \u003cp\u003eESR Spectra of Iron (III), 161\u003c\/p\u003e \u003cp\u003eIron Bioavailability, 166\u003c\/p\u003e \u003cp\u003eSiderophores, 171\u003c\/p\u003e \u003cp\u003eIron Storage and Transfer Proteins, 184\u003c\/p\u003e \u003cp\u003eFerritin, 184\u003c\/p\u003e \u003cp\u003eTransferrin, 187\u003c\/p\u003e \u003cp\u003eDioxygenase Iron Proteins, 195\u003c\/p\u003e \u003cp\u003eIron–Sulfur Proteins, 207\u003c\/p\u003e \u003cp\u003eRubredoxin, 207\u003c\/p\u003e \u003cp\u003eFerredoxins, 212\u003c\/p\u003e \u003cp\u003e2Fe–2S Ferredoxins, 212\u003c\/p\u003e \u003cp\u003e4Fe–4S Ferredoxins, 221\u003c\/p\u003e \u003cp\u003eAconitase, 226\u003c\/p\u003e \u003cp\u003eHydroxylases, 229\u003c\/p\u003e \u003cp\u003eHydrogenases, 232\u003c\/p\u003e \u003cp\u003eNitrogenases, 240\u003c\/p\u003e \u003cp\u003eBinuclear Iron Proteins, 251\u003c\/p\u003e \u003cp\u003eHemerythrin, 253\u003c\/p\u003e \u003cp\u003eRibotide Reductase, Purple Acid Phosphate, and Methane Monooxygenase, 260\u003c\/p\u003e \u003cp\u003eHemoproteins: Classification and Behavior of Heme in Absence of Globins, 267\u003c\/p\u003e \u003cp\u003eMyoglobin and Hemoglobin, 275\u003c\/p\u003e \u003cp\u003eMyoglobin, 275\u003c\/p\u003e \u003cp\u003eHemoglobin, 280\u003c\/p\u003e \u003cp\u003eCytochrome C, 298\u003c\/p\u003e \u003cp\u003eElectron Transfer in Porphyrins and Metalloporphyrins, 301\u003c\/p\u003e \u003cp\u003eCatalases, 311\u003c\/p\u003e \u003cp\u003ePeroxidases, 315\u003c\/p\u003e \u003cp\u003eCytochrome P-450, 322\u003c\/p\u003e \u003cp\u003eElectronic Spectra of Hemoproteins, 327\u003c\/p\u003e \u003cp\u003eESR Spectra of Hemoproteins, 362\u003c\/p\u003e \u003cp\u003eReferences, 378\u003c\/p\u003e \u003cp\u003e\u003cb\u003e6 Vitamin B12 393\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eReferences, 405\u003c\/p\u003e \u003cp\u003e\u003cb\u003e7 Chlorophyll 407\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eReferences, 421\u003c\/p\u003e \u003cp\u003eIndex 423\u003c\/p\u003e","brand":"John Wiley \u0026 Sons Inc","offers":[{"title":"Default Title","offer_id":49528830198103,"sku":"9781118470442","price":106.35,"currency_code":"GBP","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0817\/1739\/5799\/files\/9781118470442.jpg?v=1731873187","url":"https:\/\/bookcurl.com\/products\/chemistry-of-metalloproteins-9781118470442","provider":"Book Curl","version":"1.0","type":"link"}