LEADER 01020cam0-22003251i-450- 001 990005472230403321 005 20071023143237.0 035 $a000547223 035 $aFED01000547223 035 $a(Aleph)000547223FED01 035 $a000547223 100 $a19990604d1955----km-y0itay50------ba 101 0 $afre 102 $aFR 105 $af-------001yy 200 1 $a<>famille de marchands, les Ruiz$econtribution à l'étude du commerce entre la France et l'Espagne au temps de Philippe II$fHenri Lapeyre 210 $aParis$cA. Colin$d1955 215 $a671 p., 7 tav.$d25 cm 225 1 $aBibliothèque de l'École des hautes études hispaniques$v26 676 $a929.2 700 1$aLapeyre,$bHenri$0211697 801 0$aIT$bUNINA$gRICA$2UNIMARC 901 $aBK 912 $a990005472230403321 952 $a929.2 LAP 1$bST.MED.MOD. 1520$fFLFBC 952 $aCOLLEZ. 853 (8)$b27609$fFSPBC 959 $aFLFBC 959 $aFSPBC 996 $aFamille de marchands, les Ruiz$9587918 997 $aUNINA LEADER 04839nam 2201105z- 450 001 9910557114003321 005 20210501 035 $a(CKB)5400000000040906 035 $a(oapen)https://directory.doabooks.org/handle/20.500.12854/68459 035 $a(oapen)doab68459 035 $a(EXLCZ)995400000000040906 100 $a20202105d2021 |y 0 101 0 $aeng 135 $aurmn|---annan 181 $ctxt$2rdacontent 182 $cc$2rdamedia 183 $acr$2rdacarrier 200 00$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 $a1 online resource (186 p.) 311 08$a3-0365-0608-X 311 08$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 $aBiology, life sciences$2bicssc 606 $aResearch & information: general$2bicssc 610 $a[Fe]-hydrogenase 610 $aacetylene hydratase 610 $aaldehyde:ferredoxin oxidoreductase 610 $abenzoyl-CoA reductase 610 $acarbon assimilation 610 $aCCCP-carbonyl cyanide m-chlorophenyl-hydrazone 610 $aCO dehydrogenase 610 $aconformational changes 610 $adensity functional theory 610 $adihydrogen 610 $adithiolene ligand 610 $aEIPA-5-(N-ethyl-N-isopropyl)-amiloride 610 $aelectron transfer 610 $aelectronic structure 610 $aenergy conservation 610 $aenzyme kinetics 610 $aenzyme structure 610 $aFe-S cluster assembly 610 $aFeGP cofactor 610 $afold-angle 610 $aformate dehydrogenase 610 $aformate hydrogenlyase 610 $afrataxin 610 $aFriedreich's ataxia 610 $aguanylylpyridinol 610 $ahydrogen metabolism 610 $ahydrogenase 610 $airon 610 $airon-sulfur cluster 610 $aISC 610 $al-cysteine desulfurase 610 $amagnetic moment 610 $ametal-dithiolene 610 $ametallocofactor 610 $amixed-valence complex 610 $aMoco 610 $aMoco biosynthesis 610 $amolybdenum 610 $amolybdenum cofactor 610 $aMRP (multiple resistance and pH)-type Na+/H+ antiporter 610 $an/a 610 $anicotinamide adenine dinucleotide (NADH) 610 $aNIF 610 $apersulfide 610 $apseudo-Jahn-Teller effect 610 $apyranopterin molybdenum enzymes 610 $aquantum/classical modeling 610 $aSUF 610 $asulfur 610 $atetra-nuclear nickel complex 610 $athione 610 $atungsten cofactor 610 $atungsten enzymes 610 $aX-ray crystallography 610 $aX-ray structure 615 7$aBiology, life sciences 615 7$aResearch & information: general 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