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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| Year of Publication: | 2021 |
| Language: | English |
| Physical Description: | 1 electronic resource (186 p.) |
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| 245 | 1 | 0 | |a Transition Metals in Catalysis |b The Functional Relationship of Fe-S Clusters and Molybdenum or Tungsten Cofactor-Containing Enzyme Systems |
| 246 | |a Transition Metals in Catalysis | ||
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| 300 | |a 1 electronic resource (186 p.) | ||
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| 520 | |a 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. | ||
| 546 | |a English | ||
| 650 | 7 | |a Research & information: general |2 bicssc | |
| 650 | 7 | |a Biology, life sciences |2 bicssc | |
| 653 | |a CO dehydrogenase | ||
| 653 | |a dihydrogen | ||
| 653 | |a hydrogenase | ||
| 653 | |a quantum/classical modeling | ||
| 653 | |a density functional theory | ||
| 653 | |a metal-dithiolene | ||
| 653 | |a pyranopterin molybdenum enzymes | ||
| 653 | |a fold-angle | ||
| 653 | |a tungsten enzymes | ||
| 653 | |a electronic structure | ||
| 653 | |a pseudo-Jahn-Teller effect | ||
| 653 | |a thione | ||
| 653 | |a molybdenum cofactor | ||
| 653 | |a Moco | ||
| 653 | |a mixed-valence complex | ||
| 653 | |a dithiolene ligand | ||
| 653 | |a tetra-nuclear nickel complex | ||
| 653 | |a X-ray structure | ||
| 653 | |a magnetic moment | ||
| 653 | |a formate hydrogenlyase | ||
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| 653 | |a EIPA-5-(N-ethyl-N-isopropyl)-amiloride | ||
| 653 | |a nicotinamide adenine dinucleotide (NADH) | ||
| 653 | |a electron transfer | ||
| 653 | |a enzyme kinetics | ||
| 653 | |a enzyme structure | ||
| 653 | |a formate dehydrogenase | ||
| 653 | |a carbon assimilation | ||
| 653 | |a Moco biosynthesis | ||
| 653 | |a Fe-S cluster assembly | ||
| 653 | |a l-cysteine desulfurase | ||
| 653 | |a ISC | ||
| 653 | |a SUF | ||
| 653 | |a NIF | ||
| 653 | |a iron | ||
| 653 | |a molybdenum | ||
| 653 | |a sulfur | ||
| 653 | |a tungsten cofactor | ||
| 653 | |a aldehyde:ferredoxin oxidoreductase | ||
| 653 | |a benzoyl-CoA reductase | ||
| 653 | |a acetylene hydratase | ||
| 653 | |a [Fe]-hydrogenase | ||
| 653 | |a FeGP cofactor | ||
| 653 | |a guanylylpyridinol | ||
| 653 | |a conformational changes | ||
| 653 | |a X-ray crystallography | ||
| 653 | |a iron-sulfur cluster | ||
| 653 | |a persulfide | ||
| 653 | |a metallocofactor | ||
| 653 | |a frataxin | ||
| 653 | |a Friedreich's ataxia | ||
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| 700 | 1 | |a Magalon, Axel |4 edt | |
| 700 | 1 | |a Einsle, Oliver |4 edt | |
| 700 | 1 | |a Schulzke, Carola |4 edt | |
| 700 | 1 | |a Leimkühler, Silke |4 oth | |
| 700 | 1 | |a Magalon, Axel |4 oth | |
| 700 | 1 | |a Einsle, Oliver |4 oth | |
| 700 | 1 | |a Schulzke, Carola |4 oth | |
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