Transition Metals in Catalysis : The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems
Material type: ArticleLanguage: English Publication details: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021Description: 1 electronic resource (186 p.)ISBN:- books978-3-0365-0609-8
- 9783036506081
- 9783036506098
- Research & information: general
- Biology, life sciences
- CO dehydrogenase
- dihydrogen
- hydrogenase
- quantum/classical modeling
- density functional theory
- metal-dithiolene
- pyranopterin molybdenum enzymes
- fold-angle
- tungsten enzymes
- electronic structure
- pseudo-Jahn-Teller effect
- thione
- molybdenum cofactor
- Moco
- mixed-valence complex
- dithiolene ligand
- tetra-nuclear nickel complex
- X-ray structure
- magnetic moment
- formate hydrogenlyase
- hydrogen metabolism
- energy conservation
- MRP (multiple resistance and pH)-type Na+/H+ antiporter
- CCCP-carbonyl cyanide m-chlorophenyl-hydrazone
- EIPA-5-(N-ethyl-N-isopropyl)-amiloride
- nicotinamide adenine dinucleotide (NADH)
- electron transfer
- enzyme kinetics
- enzyme structure
- formate dehydrogenase
- carbon assimilation
- Moco biosynthesis
- Fe-S cluster assembly
- l-cysteine desulfurase
- ISC
- SUF
- NIF
- iron
- molybdenum
- sulfur
- tungsten cofactor
- aldehyde:ferredoxin oxidoreductase
- benzoyl-CoA reductase
- acetylene hydratase
- [Fe]-hydrogenase
- FeGP cofactor
- guanylylpyridinol
- conformational changes
- X-ray crystallography
- iron-sulfur cluster
- persulfide
- metallocofactor
- frataxin
- Friedreich's ataxia
- n/a
Item type | Home library | Collection | Call number | Materials specified | Status | Date due | Barcode | |
---|---|---|---|---|---|---|---|---|
Electronic-Books | OPJGU Sonepat- Campus | E-Books Open Access | Available |
Open Access star Unrestricted online access
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.
Creative Commons https://creativecommons.org/licenses/by/4.0/ cc https://creativecommons.org/licenses/by/4.0/
English
There are no comments on this title.