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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Leimkühler, Silke edt Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems Transition Metals in Catalysis Basel, Switzerland MDPI - Multidisciplinary Digital Publishing Institute 2021 1 electronic resource (186 p.) text txt rdacontent computer c rdamedia online resource cr rdacarrier 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. English Research & information: general bicssc Biology, life sciences bicssc 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 3-0365-0608-X 3-0365-0609-8 Magalon, Axel edt Einsle, Oliver edt Schulzke, Carola edt Leimkühler, Silke oth Magalon, Axel oth Einsle, Oliver oth Schulzke, Carola oth |
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English |
format |
eBook |
author2 |
Magalon, Axel Einsle, Oliver Schulzke, Carola Leimkühler, Silke Magalon, Axel Einsle, Oliver Schulzke, Carola |
author_facet |
Magalon, Axel Einsle, Oliver Schulzke, Carola Leimkühler, Silke Magalon, Axel Einsle, Oliver Schulzke, Carola |
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s l sl a m am o e oe c s cs |
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HerausgeberIn HerausgeberIn HerausgeberIn Sonstige Sonstige Sonstige Sonstige |
title |
Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
spellingShingle |
Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
title_sub |
The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
title_full |
Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
title_fullStr |
Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
title_full_unstemmed |
Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
title_auth |
Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
title_alt |
Transition Metals in Catalysis |
title_new |
Transition Metals in Catalysis |
title_sort |
transition metals in catalysis the functional relationship of fe-s clusters and molybdenum or tungsten cofactor-containing enzyme systems |
publisher |
MDPI - Multidisciplinary Digital Publishing Institute |
publishDate |
2021 |
physical |
1 electronic resource (186 p.) |
isbn |
3-0365-0608-X 3-0365-0609-8 |
illustrated |
Not Illustrated |
work_keys_str_mv |
AT leimkuhlersilke transitionmetalsincatalysisthefunctionalrelationshipoffesclustersandmolybdenumortungstencofactorcontainingenzymesystems AT magalonaxel transitionmetalsincatalysisthefunctionalrelationshipoffesclustersandmolybdenumortungstencofactorcontainingenzymesystems AT einsleoliver transitionmetalsincatalysisthefunctionalrelationshipoffesclustersandmolybdenumortungstencofactorcontainingenzymesystems AT schulzkecarola transitionmetalsincatalysisthefunctionalrelationshipoffesclustersandmolybdenumortungstencofactorcontainingenzymesystems AT leimkuhlersilke transitionmetalsincatalysis AT magalonaxel transitionmetalsincatalysis AT einsleoliver transitionmetalsincatalysis AT schulzkecarola transitionmetalsincatalysis |
status_str |
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(CKB)5400000000040906 (oapen)https://directory.doabooks.org/handle/20.500.12854/68459 (EXLCZ)995400000000040906 |
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Transition Metals in Catalysis The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
author2_original_writing_str_mv |
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