TY  - GEN
AU  - Leimkühler,Silke
AU  - Magalon,Axel
AU  - Einsle,Oliver
AU  - Schulzke,Carola
AU  - Leimkühler,Silke
AU  - Magalon,Axel
AU  - Einsle,Oliver
AU  - Schulzke,Carola
TI  - Transition Metals in Catalysis : The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems
SN  - books978-3-0365-0609-8
PY  - 2021///
CY  - Basel, Switzerland
PB  - MDPI - Multidisciplinary Digital Publishing Institute
KW  - Research & information: general
KW  - bicssc
KW  - Biology, life sciences
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
N1  - Open Access
N2  - 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
UR  - https://mdpi.com/books/pdfview/book/3477
UR  - https://directory.doabooks.org/handle/20.500.12854/68459
ER  -