TY - BOOK ID - 136443533 TI - Transition Metals in Catalysis : The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems AU - Leimkühler, Silke AU - Magalon, Axel AU - Einsle, Oliver AU - Schulzke, Carola PY - 2021 PB - Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute DB - UniCat KW - CO dehydrogenase KW - dihydrogen KW - hydrogenase KW - quantum/classical modeling KW - density functional theory KW - metal–dithiolene KW - pyranopterin molybdenum enzymes KW - fold-angle KW - tungsten enzymes KW - electronic structure KW - pseudo-Jahn–Teller effect KW - thione KW - molybdenum cofactor KW - Moco KW - mixed-valence complex KW - dithiolene ligand KW - tetra-nuclear nickel complex KW - X-ray structure KW - magnetic moment KW - formate hydrogenlyase KW - hydrogen metabolism KW - energy conservation KW - MRP (multiple resistance and pH)-type Na+/H+ antiporter KW - CCCP—carbonyl cyanide m-chlorophenyl-hydrazone KW - EIPA—5-(N-ethyl-N-isopropyl)-amiloride KW - nicotinamide adenine dinucleotide (NADH) KW - electron transfer KW - enzyme kinetics KW - enzyme structure KW - formate dehydrogenase KW - carbon assimilation KW - Moco biosynthesis KW - Fe-S cluster assembly KW - l-cysteine desulfurase KW - ISC KW - SUF KW - NIF KW - iron KW - molybdenum KW - sulfur KW - tungsten cofactor KW - aldehyde:ferredoxin oxidoreductase KW - benzoyl-CoA reductase KW - acetylene hydratase KW - [Fe]-hydrogenase KW - FeGP cofactor KW - guanylylpyridinol KW - conformational changes KW - X-ray crystallography KW - iron-sulfur cluster KW - persulfide KW - metallocofactor KW - frataxin KW - Friedreich’s ataxia KW - n/a KW - metal-dithiolene KW - pseudo-Jahn-Teller effect KW - CCCP-carbonyl cyanide m-chlorophenyl-hydrazone KW - EIPA-5-(N-ethyl-N-isopropyl)-amiloride KW - Friedreich's ataxia UR - https://www.unicat.be/uniCat?func=search&query=sysid:136443533 AB - 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. ER -