{"product_id":"metalloprotein-active-site-assembly-isbn-9781119159834","title":"Metalloprotein Active Site Assembly","description":"\u003cp\u003e\u003cb\u003eSummarizes the essential biosynthetic pathways for assembly of metal cofactor sites in functional metalloproteins\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003e\u003ci\u003eMetalloprotein Active Site Assembly\u003c\/i\u003e focuses on the processes that have evolved to orchestrate the assembly of metal cofactor sites in functional metalloproteins. It goes beyond the simple incorporation of single metal ions in a protein framework, and includes metal cluster assembly, metal-cofactor biosynthesis and insertion, and metal-based post-translational modifications of the protein environments that are necessary for function. Several examples of each of these areas have now been identified and studied; the current volume provides the current state-of-the-art understanding of the processes involved.\u003c\/p\u003e \u003cp\u003eAn excellent companion to the earlier book in this series\u003ci\u003e Metals in Cells\u003c\/i\u003e—which discussed both the positive and negative effects of cellular interactions with metals—this comprehensive book provides a diverse sampling of what is known about metalloprotein active site assembly processes. It covers all major biological transition metal components (Mn, Fe, Co, Ni, Mo), as well as the other inorganic components, metal-binding organic cofactors (e.g., heme, siroheme, cobalamin, molybdopterin), and post-translationally modified metal binding sites that make up the patchwork of evolved biological catalytic sites. The book compares and contrasts the biosynthetic assembly of active sites involving all biological metals. This has never been done before since it is a relatively new, fast-developing area of research.\u003c\/p\u003e \u003cp\u003e\u003ci\u003eMetalloprotein Active Site Assembly\u003c\/i\u003e is an ideal text for practitioners of inorganic biochemistry who are studying the biosynthetic pathways and gene clusters involved in active site assembly, and for inorganic chemists who want to apply the concepts learned to potential synthetic pathways to active site mimics.\u003c\/p\u003e \u003cp\u003eContributors ix\u003c\/p\u003e \u003cp\u003eSeries Preface xiii\u003c\/p\u003e \u003cp\u003eVolume Preface xv\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 1: Assembly and Trafficking of Simple Fe-S Clusters 1\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eNif System for Simple [Fe–S] Cluster Assembly in Nitrogen-Fixing Bacteria 3\u003cbr\u003e\u003ci\u003ePatricia C. Dos Santos and Dennis R. Dean\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIron–Sulfur Cluster Assembly in Bacteria and Eukarya using the ISC Biosynthesis Machinery 17\u003cbr\u003e\u003ci\u003eSandrine Ollagnier de Choudens and Hélène Puccio\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eThe Suf System in Archaea, Bacteria, and Eukaryotic Organelles 37\u003cbr\u003e\u003ci\u003eGuangchao Dong, Savannah Witcher, F. Wayne Outten and Marinus Pilon\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eRoles of Class II Glutaredoxins in the Maturation of Fe–S Proteins 53\u003cbr\u003e\u003ci\u003eJonathan Przybyla-Toscano, Thomas Roret, Jérémy Couturier and Nicolas Rouhier\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 2: Assembly of Complex and Heterometallic Fe-S Cluster Active Sites 73\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eNitrogenase Metallocluster Assembly 75\u003cbr\u003e\u003ci\u003eNathaniel S. Sickerman, Lee A. Rettberg, Yilin Hu and Markus W. Ribbe\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eMetallocluster Assembly: Maturation of [FeFe]-Hydrogenases 93\u003cbr\u003e\u003ci\u003eGiorgio Caserta, Ludovic Pecqueur, Cecilia Papini and Marc Fontecave\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eCO Dehydrogenase and Acetyl-CoA Synthase 111\u003cbr\u003e\u003ci\u003eHolger Dobbek\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 3: Assembly of Homometallic and Heterometalic Cu Cluster Active Sites 123\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eAssembly of Dinuclear Copper Center in Tyrosinases and Hemocyanins 125\u003cbr\u003e\u003ci\u003eNobutaka Fujieda and Shinobu Itoh\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eMulticopper Oxidases 139\u003cbr\u003e\u003ci\u003eDaniel J. Kosman\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eAssembly of the Redox-Active Metal Centers of Cytochrome \u003ci\u003ec \u003c\/i\u003eOxidase 157\u003cbr\u003e\u003ci\u003eEva Nyvltova, Antoni Barrientos and Jonathan Hosler\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eCuA and CuZ Center Assembly in Nitrous Oxide Reductase 185\u003cbr\u003e\u003ci\u003eSofia R. Pauleta and Isabel Moura\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eMoCu CO Dehydrogenase and its Active-Site Assembly 197\u003cbr\u003e\u003ci\u003eFrank Mickoleit\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 4: Assembly of Homometallic and Heterometallic Mn Clusters 213\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eHomo- and Heterometallic Dinuclear Manganese Proteins: Active Site Assembly 215\u003cbr\u003e\u003ci\u003eGustav Berggren, Daniel Lundin and Britt-Marie Sjöberg\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eBiogenesis and Assembly of the CaMn\u003csub\u003e4\u003c\/sub\u003eO\u003csub\u003e5\u003c\/sub\u003e Core of Photosynthetic Water Oxidases and Inorganic Mutants 233\u003cbr\u003e\u003ci\u003eColin Gates, Gennady Ananyev and G. Charles Dismukes\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 5: Assembly of Homometallic and Heterometallic Ni Clusters 249\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eUrease Activation 251\u003cbr\u003e\u003ci\u003eRobert P. Hausinger\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eInsights into [NiFe]-Hydrogenase Active Site Metallocluster Assembly 261\u003cbr\u003e\u003ci\u003eRobert Gary Sawers and Constanze Pinske\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003e\u003cb\u003ePart 6: Assembly of Cofactors for Binding Active-Site Metal Centers 273\u003c\/b\u003e\u003c\/p\u003e \u003cp\u003eMoco in Mo\/W Enzymes 275\u003cbr\u003e\u003ci\u003eSilke Leimkühler\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eHeme Biosynthesis 299\u003cbr\u003e\u003ci\u003eAmy E. Medlock and Harry A. Dailey\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eSiroheme Assembly and Insertion to Nitrite and Sulfite Reductase 315\u003cbr\u003e\u003ci\u003eM. Elizabeth Stroupe and Martin J. Warren\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eBiosynthesis of Coenzyme F430 and the Posttranslational Modification of the Active Site Region of Methyl-Coenzyme M Reductase 323\u003cbr\u003e\u003ci\u003eSteven O. Mansoorabadi, Kaiyuan Zheng and Phong D. Ngo\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eCoenzyme B12 Biosynthesis in Bacteria and Archaea 335\u003cbr\u003e\u003ci\u003eTheodoric A. Mattes, Jorge C. Escalante-Semerena, Evelyne Deery and Martin J. Warren\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eCrosslinked Cys–Tyr Free Radical Redox Cofactor 361\u003cbr\u003e\u003ci\u003eJames W. Whittaker\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eTopaquinone Biogenesis and Lysyl Tyrosine Quinone Biogenesis in Cu Amine Oxidases 375\u003cbr\u003e\u003ci\u003eDavid M. Dooley, Doreen E. Brown and Eric M. Shepard\u003c\/i\u003e\u003c\/p\u003e \u003cp\u003eIndex 389\u003c\/p\u003e   \u003cp\u003eEditors\u003cbr\u003e   \u003cstrong\u003eMichael K. Johnson,\u003c\/strong\u003e \u003cem\u003eUniversity of Georgia, Athens, GA, USA\u003c\/em\u003e\u003cbr\u003e   \u003cstrong\u003eRobert A. Scott,\u003c\/strong\u003e \u003cem\u003eUniversity of Georgia, Athens, GA, USA\u003c\/em\u003e      \u003c\/p\u003e\u003cp\u003e \u003cstrong\u003eSummarizes the essential biosynthetic pathways for assembly of metal cofactor sites in functional metalloproteins\u003c\/strong\u003e   \u003c\/p\u003e\u003cp\u003e \u003cem\u003eMetalloprotein Active Site Assembly\u003c\/em\u003e focuses on the processes that have evolved to orchestrate the assembly of metal cofactor sites in functional metalloproteins. It goes beyond the simple incorporation of single metal ions in a protein framework, and includes metal cluster assembly, metal-cofactor biosynthesis and insertion, and metal-based post-translational modifications of the protein environments that are necessary for function. Several examples of each of these areas have now been identified and studied; the current volume provides the current state-of-the-art understanding of the processes involved.    \u003c\/p\u003e\u003cp\u003e An excellent companion to the earlier book in this series \u003cem\u003eMetals in Cells\u003c\/em\u003e—which discussed both the positive and negative effects of cellular interactions with metals—this comprehensive book provides a diverse sampling of what is known about metalloprotein active site assembly processes. It covers all major biological transition metal components (Mn, Fe, Co, Ni, Mo), as well as the other inorganic components, metal-binding organic cofactors (e.g., heme, siroheme, cobalamin, molybdopterin), and post-translationally modified metal binding sites that make up the patchwork of evolved biological catalytic sites. The book compares and contrasts the biosynthetic assembly of active sites involving all biological metals. This has never been done before since it is a relatively new, fast-developing area of research.   \u003c\/p\u003e\u003cp\u003e\u003cem\u003eMetalloprotein Active Site Assembly\u003c\/em\u003e is an ideal text for practitioners of inorganic biochemistry who are studying the biosynthetic pathways and gene clusters involved in active site assembly, and for inorganic chemists who want to apply the concepts learned to potential synthetic pathways to active site mimics.   \u003c\/p\u003e\u003cp\u003e About \u003cstrong\u003eEIBC Books\u003c\/strong\u003e   \u003c\/p\u003e\u003cp\u003eThe \u003cstrong\u003eEncyclopedia of Inorganic and Bioinorganic Chemistry (EIBC)\u003c\/strong\u003e was created as an online reference in 2012 by merging the \u003cem\u003eEncyclopedia of Inorganic Chemistry\u003c\/em\u003e and the \u003cem\u003eHandbook of Metalloproteins.\u003c\/em\u003e The resulting combination proves to be the defining reference work in the field of inorganic and bioinorganic chemistry, and a lot of chemistry libraries around the world have access to the online version. Many readers, however, prefer to have more concise thematic volumes in print, targeted to their specific area of interest. This feedback from EIBC readers has encouraged the Editors to plan a series of EIBC Books [formerly called EIC Books], focusing on topics of current interest.   \u003c\/p\u003e\u003cp\u003eEIBC Books will appear on a regular basis, will be edited by the EIBC Editors and specialist Guest Editors, and will feature articles from leading scholars in their fields. EIBC Books aim to provide both the starting research student and the confirmed research worker with a critical distillation of the leading concepts in inorganic and bioinorganic chemistry, and provide a structured entry into the fields covered.\u003c\/p\u003e","brand":"Wiley","offers":[{"title":"Default Title","offer_id":47989612839141,"sku":"NP9781119159834","price":206.95,"currency_code":"USD","in_stock":false}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/1842\/7735\/files\/9781119159834.jpg?v=1761784808","url":"https:\/\/k12savings.com\/es\/products\/metalloprotein-active-site-assembly-isbn-9781119159834","provider":"K12savings","version":"1.0","type":"link"}