04839nam 2201105z- 450 991055711400332120210501(CKB)5400000000040906(oapen)https://directory.doabooks.org/handle/20.500.12854/68459(oapen)doab68459(EXLCZ)99540000000004090620202105d2021 |y 0engurmn|---annantxtrdacontentcrdamediacrrdacarrierTransition Metals in CatalysisThe Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme SystemsBasel, SwitzerlandMDPI - Multidisciplinary Digital Publishing Institute20211 online resource (186 p.)3-0365-0608-X 3-0365-0609-8 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.Transition Metals in Catalysis Biology, life sciencesbicsscResearch & information: generalbicssc[Fe]-hydrogenaseacetylene hydratasealdehyde:ferredoxin oxidoreductasebenzoyl-CoA reductasecarbon assimilationCCCP-carbonyl cyanide m-chlorophenyl-hydrazoneCO dehydrogenaseconformational changesdensity functional theorydihydrogendithiolene ligandEIPA-5-(N-ethyl-N-isopropyl)-amilorideelectron transferelectronic structureenergy conservationenzyme kineticsenzyme structureFe-S cluster assemblyFeGP cofactorfold-angleformate dehydrogenaseformate hydrogenlyasefrataxinFriedreich's ataxiaguanylylpyridinolhydrogen metabolismhydrogenaseironiron-sulfur clusterISCl-cysteine desulfurasemagnetic momentmetal-dithiolenemetallocofactormixed-valence complexMocoMoco biosynthesismolybdenummolybdenum cofactorMRP (multiple resistance and pH)-type Na+/H+ antiportern/anicotinamide adenine dinucleotide (NADH)NIFpersulfidepseudo-Jahn-Teller effectpyranopterin molybdenum enzymesquantum/classical modelingSUFsulfurtetra-nuclear nickel complexthionetungsten cofactortungsten enzymesX-ray crystallographyX-ray structureBiology, life sciencesResearch & information: generalLeimkühler Silkeedt0Magalon AxeledtEinsle OliveredtSchulzke CarolaedtLeimkühler SilkeothMagalon AxelothEinsle OliverothSchulzke CarolaothBOOK9910557114003321Transition Metals in Catalysis3025251UNINA