Transition Metals in Catalysis : The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems

• Autore: Leimkühler Silke
• Pubblicazione: Basel, Switzerland, : MDPI - Multidisciplinary Digital Publishing Institute, 2021
• Descrizione fisica: 1 online resource (186 p.)
• Soggetto topico: Biology, life sciences; Research & information: general
• Soggetto non controllato: [Fe]-hydrogenase; acetylene hydratase; aldehyde:ferredoxin oxidoreductase; benzoyl-CoA reductase; carbon assimilation; CCCP-carbonyl cyanide m-chlorophenyl-hydrazone; CO dehydrogenase; conformational changes; density functional theory; dihydrogen; dithiolene ligand; EIPA-5-(N-ethyl-N-isopropyl)-amiloride; electron transfer; electronic structure; energy conservation; enzyme kinetics; enzyme structure; Fe-S cluster assembly; FeGP cofactor; fold-angle; formate dehydrogenase; formate hydrogenlyase; frataxin; Friedreich's ataxia; guanylylpyridinol; hydrogen metabolism; hydrogenase; iron; iron-sulfur cluster; ISC; l-cysteine desulfurase; magnetic moment; metal-dithiolene; metallocofactor; mixed-valence complex; Moco; Moco biosynthesis; molybdenum; molybdenum cofactor; MRP (multiple resistance and pH)-type Na+/H+ antiporter; n/a; nicotinamide adenine dinucleotide (NADH); NIF; persulfide; pseudo-Jahn-Teller effect; pyranopterin molybdenum enzymes; quantum/classical modeling; SUF; sulfur; tetra-nuclear nickel complex; thione; tungsten cofactor; tungsten enzymes; X-ray crystallography; X-ray structure
• Persona (resp. second.): MagalonAxel; EinsleOliver; SchulzkeCarola; LeimkühlerSilke
• Sommario/riassunto: Iron-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.
• Altri titoli varianti: Transition Metals in Catalysis
• Titolo autorizzato: Transition Metals in Catalysis
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Lingua di pubblicazione: Inglese
• Record Nr.: 9910557114003321
• Lo trovi qui: Univ. Federico II