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Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems

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-con...

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Bibliographic Details
Main Author: Leimkühler, Silke
Other Authors: Magalon, Axel, Einsle, Oliver, Schulzke, Carola
Format: eBook
Language:English
Published: Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021
Subjects:
Persulfide
Pyranopterin Molybdenum Enzymes
Fegp Cofactor
Suf
Metal-dithiolene
Fe-s Cluster Assembly
N/a
Benzoyl-coa Reductase
Enzyme Kinetics
Electron Transfer
Density Functional Theory
Carbon Assimilation
Frataxin
X-ray Structure
Co Dehydrogenase
Formate Dehydrogenase
Enzyme Structure
[fe]-hydrogenase
Pseudo-jahn-teller Effect
L-cysteine Desulfurase
Dithiolene Ligand
Cccp-carbonyl Cyanide M-chlorophenyl-hydrazone
Acetylene Hydratase
Tungsten Enzymes
Moco
Fold-angle
Moco Biosynthesis
Energy Conservation
Mixed-valence Complex
Thione
Iron-sulfur Cluster
Research & Information: General / Bicssc
Guanylylpyridinol
Biology, Life Sciences / Bicssc
Hydrogenase
Tungsten Cofactor
Molybdenum Cofactor
Sulfur
Conformational Changes
Friedreich's Ataxia
Iron
Mrp (multiple Resistance And Ph)-type Na+/h+ Antiporter
Isc
Nicotinamide Adenine Dinucleotide (nadh)
Nif
Metallocofactor
Magnetic Moment
Quantum/classical Modeling
Tetra-nuclear Nickel Complex
Aldehyde:ferredoxin Oxidoreductase
Hydrogen Metabolism
Eipa-5-(n-ethyl-n-isopropyl)-amiloride
Dihydrogen
Formate Hydrogenlyase
Molybdenum
X-ray Crystallography
Electronic Structure
Online Access:
Collection: Directory of Open Access Books - Collection details see MPG.ReNa
Description
Summary: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.
Item Description:Creative Commons (cc), https://creativecommons.org/licenses/by/4.0/
Physical Description:1 electronic resource (186 p.)
ISBN:9783036506081
books978-3-0365-0609-8
9783036506098

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