Transition Metals in Catalysis

The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems

Edited by
March 2021
186 pages
  • ISBN978-3-0365-0608-1 (Hardback)
  • ISBN978-3-0365-0609-8 (PDF)

This book is a reprint of the Special Issue Transition Metals in Catalysis: The Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems that was published in

Chemistry & Materials Science
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.
  • Hardback
License and Copyright
© 2022 by the authors; CC BY-NC-ND license
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 enzymes; tungsten cofactor; aldehyde:ferredoxin oxidoreductase; benzoyl-CoA reductase; acetylene hydratase; formate dehydrogenase; [Fe]-hydrogenase; FeGP cofactor; guanylylpyridinol; conformational changes; X-ray crystallography; iron; sulfur; iron-sulfur cluster; persulfide; metallocofactor; ISC; SUF; NIF; frataxin; Friedreich’s ataxia; n/a

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