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dc.contributor.editorLeimkühler, Silke
dc.contributor.editorMagalon, Axel
dc.contributor.editorEinsle, Oliver
dc.contributor.editorSchulzke, Carola
dc.date.accessioned2021-05-01T15:10:36Z
dc.date.available2021-05-01T15:10:36Z
dc.date.issued2021
dc.identifierONIX_20210501_9783036506081_205
dc.identifier.urihttps://directory.doabooks.org/handle/20.500.12854/68459
dc.description.abstractIron–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.
dc.languageEnglish
dc.subject.classificationthema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: generalen_US
dc.subject.classificationthema EDItEUR::P Mathematics and Science::PS Biology, life sciencesen_US
dc.subject.otherCO dehydrogenase
dc.subject.otherdihydrogen
dc.subject.otherhydrogenase
dc.subject.otherquantum/classical modeling
dc.subject.otherdensity functional theory
dc.subject.othermetal–dithiolene
dc.subject.otherpyranopterin molybdenum enzymes
dc.subject.otherfold-angle
dc.subject.othertungsten enzymes
dc.subject.otherelectronic structure
dc.subject.otherpseudo-Jahn–Teller effect
dc.subject.otherthione
dc.subject.othermolybdenum cofactor
dc.subject.otherMoco
dc.subject.othermixed-valence complex
dc.subject.otherdithiolene ligand
dc.subject.othertetra-nuclear nickel complex
dc.subject.otherX-ray structure
dc.subject.othermagnetic moment
dc.subject.otherformate hydrogenlyase
dc.subject.otherhydrogen metabolism
dc.subject.otherenergy conservation
dc.subject.otherMRP (multiple resistance and pH)-type Na+/H+ antiporter
dc.subject.otherCCCP—carbonyl cyanide m-chlorophenyl-hydrazone
dc.subject.otherEIPA—5-(N-ethyl-N-isopropyl)-amiloride
dc.subject.othernicotinamide adenine dinucleotide (NADH)
dc.subject.otherelectron transfer
dc.subject.otherenzyme kinetics
dc.subject.otherenzyme structure
dc.subject.otherformate dehydrogenase
dc.subject.othercarbon assimilation
dc.subject.otherMoco biosynthesis
dc.subject.otherFe-S cluster assembly
dc.subject.otherl-cysteine desulfurase
dc.subject.otherISC
dc.subject.otherSUF
dc.subject.otherNIF
dc.subject.otheriron
dc.subject.othermolybdenum
dc.subject.othersulfur
dc.subject.othertungsten cofactor
dc.subject.otheraldehyde:ferredoxin oxidoreductase
dc.subject.otherbenzoyl-CoA reductase
dc.subject.otheracetylene hydratase
dc.subject.other[Fe]-hydrogenase
dc.subject.otherFeGP cofactor
dc.subject.otherguanylylpyridinol
dc.subject.otherconformational changes
dc.subject.otherX-ray crystallography
dc.subject.otheriron-sulfur cluster
dc.subject.otherpersulfide
dc.subject.othermetallocofactor
dc.subject.otherfrataxin
dc.subject.otherFriedreich’s ataxia
dc.subject.othern/a
dc.titleTransition Metals in Catalysis
dc.title.alternativeThe Functional Relationship of Fe–S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems
dc.typebook
oapen.identifier.doi10.3390/books978-3-0365-0609-8
oapen.relation.isPublishedBy46cabcaa-dd94-4bfe-87b4-55023c1b36d0
oapen.relation.isbn9783036506081
oapen.relation.isbn9783036506098
oapen.pages186
oapen.place.publicationBasel, Switzerland


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