{"product_id":"transition-metals-in-catalysis-the-functional-relationship-of-fe-s-clusters-and-molybdenum-or-tungsten-cofactor-containing-enzyme-systems-hardcover","title":"Transition Metals in Catalysis: The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems - Hardcover","description":"\u003cdiv\u003e\u003cp style=\"text-align: right;\"\u003e\u003ca href=\"https:\/\/reportcopyrightinfringement.com\/\" target=\"_blank\" rel=\"nofollow\"\u003e\u003cb\u003eReport copyright infringement\u003c\/b\u003e\u003c\/a\u003e\u003c\/p\u003e\u003c\/div\u003e\u003cp\u003eby \u003cb\u003eSilke Leimkühler\u003c\/b\u003e (Guest Editor), \u003cb\u003eAxel Magalon\u003c\/b\u003e (Guest Editor), \u003cb\u003eOliver Einsle\u003c\/b\u003e (Guest Editor)\u003c\/p\u003e\u003cp\u003e\u003c\/p\u003e\u003cp\u003eIron-sulfur (FeS) centers are essential protein cofactors in all forms of life. They are involved in many key biological processes. In particular, Fe-S centers not only serve as enzyme cofactors in catalysis and electron transfer, they are also indispensable for the biosynthesis of complex metal-containing cofactors. Among these cofactors are the molybdenum (Moco) and tungsten (Wco) cofactors. Both Moco\/Wco biosynthesis and Fe-S cluster assembly are highly conserved among all kingdoms of life. After formation, Fe-S clusters are transferred to carrier proteins, which insert them into recipient apo-proteins. Moco\/Wco cofactors are composed of a tricyclic pterin compound, with the metal coordinated to its unique dithiolene group. Moco\/Wco biosynthesis starts with an Fe-S cluster-dependent step involving radical\/S-adenosylmethionine (SAM) chemistry. The current lack of knowledge of the connection of the assembly\/biosynthesis of complex metal-containing cofactors is due to the sheer complexity of their synthesis with regard to both the (genetic) regulation and (chemical) metal center assembly. Studies on these metal-cofactors\/cofactor-containing enzymes are important for understanding fundamental cellular processes. They will also provide a comprehensive view of the complex biosynthesis and the catalytic mechanism of metalloenzymes that underlie metal-related human diseases.\u003c\/p\u003e\n            \u003cdiv\u003e\n\u003cstrong\u003eNumber of Pages:\u003c\/strong\u003e 186\u003c\/div\u003e\n            \u003cdiv\u003e\n\u003cstrong\u003eDimensions:\u003c\/strong\u003e 0.63 x 9.61 x 6.69 IN\u003c\/div\u003e\n            \u003cdiv\u003e\n\u003cstrong\u003ePublication Date:\u003c\/strong\u003e March 10, 2021\u003c\/div\u003e\n            ","brand":"BooksCloud","offers":[{"title":"Default Title","offer_id":53213376839987,"sku":"9783036506081","price":70.83,"currency_code":"USD","in_stock":true}],"thumbnail_url":"\/\/cdn.shopify.com\/s\/files\/1\/0300\/5595\/6612\/files\/AD140TmDvI9783036506081.webp?v=1775764102","url":"https:\/\/www.vysn.com\/en-ca\/products\/transition-metals-in-catalysis-the-functional-relationship-of-fe-s-clusters-and-molybdenum-or-tungsten-cofactor-containing-enzyme-systems-hardcover","provider":"VYSN","version":"1.0","type":"link"}