Transition Metals in Catalysis
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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MDPI - Multidisciplinary Digital Publishing Institute
2021
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| description | 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. |
| format | Online |
| id | doab-20.500.12854ir-68459 |
| institution | Directory of Open Access Books |
| language | eng |
| publishDate | 2021 |
| publishDateRange | 2021 |
| publishDateSort | 2021 |
| publisher | MDPI - Multidisciplinary Digital Publishing Institute |
| publisherStr | MDPI - Multidisciplinary Digital Publishing Institute |
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| spelling | doab-20.500.12854ir-684592024-03-28T03:33:12Z Transition Metals in Catalysis Leimkühler, Silke Magalon, Axel Einsle, Oliver Schulzke, Carola 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences 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. 2021-05-01T15:10:36Z 2021-05-01T15:10:36Z 2021 book ONIX_20210501_9783036506081_205 9783036506081 9783036506098 https://directory.doabooks.org/handle/20.500.12854/68459 eng application/octet-stream Attribution 4.0 International https://mdpi.com/books/pdfview/book/3477 https://mdpi.com/books/pdfview/book/3477 MDPI - Multidisciplinary Digital Publishing Institute 10.3390/books978-3-0365-0609-8 10.3390/books978-3-0365-0609-8 46cabcaa-dd94-4bfe-87b4-55023c1b36d0 9783036506081 9783036506098 186 Basel, Switzerland open access |
| spellingShingle | 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences Transition Metals in Catalysis |
| title | Transition Metals in Catalysis |
| title_full | Transition Metals in Catalysis |
| title_fullStr | Transition Metals in Catalysis |
| title_full_unstemmed | Transition Metals in Catalysis |
| title_short | Transition Metals in Catalysis |
| title_sort | transition metals in catalysis |
| topic | 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| topic_facet | 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 n/a thema EDItEUR::G Reference, Information and Interdisciplinary subjects::GP Research and information: general thema EDItEUR::P Mathematics and Science::PS Biology, life sciences |
| url | ONIX_20210501_9783036506081_205 |