LEADER 04804nam 2201081z- 450 001 9910557114003321 005 20231214133651.0 035 $a(CKB)5400000000040906 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/68459 035 $a(EXLCZ)995400000000040906 100 $a20202105d2021 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 10$aTransition Metals in Catalysis$eThe Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems 210 $aBasel, Switzerland$cMDPI - Multidisciplinary Digital Publishing Institute$d2021 215 $a1 electronic resource (186 p.) 311 $a3-0365-0608-X 311 $a3-0365-0609-8 330 $aIron?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. 517 $aTransition Metals in Catalysis 606 $aResearch & information: general$2bicssc 606 $aBiology, life sciences$2bicssc 610 $aCO dehydrogenase 610 $adihydrogen 610 $ahydrogenase 610 $aquantum/classical modeling 610 $adensity functional theory 610 $ametal-dithiolene 610 $apyranopterin molybdenum enzymes 610 $afold-angle 610 $atungsten enzymes 610 $aelectronic structure 610 $apseudo-Jahn-Teller effect 610 $athione 610 $amolybdenum cofactor 610 $aMoco 610 $amixed-valence complex 610 $adithiolene ligand 610 $atetra-nuclear nickel complex 610 $aX-ray structure 610 $amagnetic moment 610 $aformate hydrogenlyase 610 $ahydrogen metabolism 610 $aenergy conservation 610 $aMRP (multiple resistance and pH)-type Na+/H+ antiporter 610 $aCCCP-carbonyl cyanide m-chlorophenyl-hydrazone 610 $aEIPA-5-(N-ethyl-N-isopropyl)-amiloride 610 $anicotinamide adenine dinucleotide (NADH) 610 $aelectron transfer 610 $aenzyme kinetics 610 $aenzyme structure 610 $aformate dehydrogenase 610 $acarbon assimilation 610 $aMoco biosynthesis 610 $aFe-S cluster assembly 610 $al-cysteine desulfurase 610 $aISC 610 $aSUF 610 $aNIF 610 $airon 610 $amolybdenum 610 $asulfur 610 $atungsten cofactor 610 $aaldehyde:ferredoxin oxidoreductase 610 $abenzoyl-CoA reductase 610 $aacetylene hydratase 610 $a[Fe]-hydrogenase 610 $aFeGP cofactor 610 $aguanylylpyridinol 610 $aconformational changes 610 $aX-ray crystallography 610 $airon-sulfur cluster 610 $apersulfide 610 $ametallocofactor 610 $afrataxin 610 $aFriedreich's ataxia 615 7$aResearch & information: general 615 7$aBiology, life sciences 700 $aLeimku?hler$b Silke$4edt$00 702 $aMagalon$b Axel$4edt 702 $aEinsle$b Oliver$4edt 702 $aSchulzke$b Carola$4edt 702 $aLeimku?hler$b Silke$4oth 702 $aMagalon$b Axel$4oth 702 $aEinsle$b Oliver$4oth 702 $aSchulzke$b Carola$4oth 906 $aBOOK 912 $a9910557114003321 996 $aTransition Metals in Catalysis$93025251 997 $aUNINA