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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues
Print on DemandSeller: BuchWeltWeit Ludwig Meier e.K., Bergisch Gladbach, Germany
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Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in recent years. This work uses synthetic [2Fe-2S] analogues to explore the role alternative ligands play in determining the reactivity of iron sulfur clusters. Isomerization in a homoleptically coordinated cluster utilizing a mixed nitrogen- and sulfur-donating ligand is investigated as a model for ligand rearrangement processes during iron sulfur cluster biogenesis. Furthermore, a high fidelity model system for the asymmetrically ligated [2Fe-2S] cluster of mitoNEET proteins is developed and characterized in detail. This cluster and its homoleptic analogue are studied as reagents in proton coupled electron transfer processes, highlighting the role asymmetry and reorganization energy play in tuning this reactivity. The effects of the ligation pattern on entropic contributions during reduction are probed by temperature dependent electrochemical measurements. Finally, synthetic [2Fe-2S] clusters are investigated with respect to their reactivity with organic radicals, mimicking the unique reactivity of biotin synthase. 198 pp. Englisch. Seller Inventory # 9783736996724
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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands
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Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. KlappentextrnrnIron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so. Seller Inventory # 199862354
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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues
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Cuvillier, Cuvillier Dez 2017, 2017
ISBN 10: 3736996721
ISBN 13: 9783736996724
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Seller: buchversandmimpf2000, Emtmannsberg, BAYE, Germany
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Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in recent years. This work uses synthetic [2Fe-2S] analogues to explore the role alternative ligands play in determining the reactivity of iron sulfur clusters. Isomerization in a homoleptically coordinated cluster utilizing a mixed nitrogen- and sulfur-donating ligand is investigated as a model for ligand rearrangement processes during iron sulfur cluster biogenesis. Furthermore, a high fidelity model system for the asymmetrically ligated [2Fe-2S] cluster of mitoNEET proteins is developed and characterized in detail. This cluster and its homoleptic analogue are studied as reagents in proton coupled electron transfer processes, highlighting the role asymmetry and reorganization energy play in tuning this reactivity. The effects of the ligation pattern on entropic contributions during reduction are probed by temperature dependent electrochemical measurements. Finally, synthetic [2Fe-2S] clusters are investigated with respect to their reactivity with organic radicals, mimicking the unique reactivity of biotin synthase.Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen 198 pp. Englisch. Seller Inventory # 9783736996724
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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues
Print on DemandSeller: AHA-BUCH GmbH, Einbeck, Germany
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Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Iron sulfur clusters are essential cofactors involved in electron transfer, sensing, and catalysis in all three kingdoms of life. While most iron sulfur clusters are ligated by cysteine thiolates, a number of clusters featuring so called alternative ligands such as histidine have been recognized in recent years. This work uses synthetic [2Fe-2S] analogues to explore the role alternative ligands play in determining the reactivity of iron sulfur clusters. Isomerization in a homoleptically coordinated cluster utilizing a mixed nitrogen- and sulfur-donating ligand is investigated as a model for ligand rearrangement processes during iron sulfur cluster biogenesis. Furthermore, a high fidelity model system for the asymmetrically ligated [2Fe-2S] cluster of mitoNEET proteins is developed and characterized in detail. This cluster and its homoleptic analogue are studied as reagents in proton coupled electron transfer processes, highlighting the role asymmetry and reorganization energy play in tuning this reactivity. The effects of the ligation pattern on entropic contributions during reduction are probed by temperature dependent electrochemical measurements. Finally, synthetic [2Fe-2S] clusters are investigated with respect to their reactivity with organic radicals, mimicking the unique reactivity of biotin synthase. Seller Inventory # 9783736996724
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Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues
Print on DemandSeller: preigu, Osnabrück, Germany
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Taschenbuch. Condition: Neu. Biomimetic Function of Iron Sulfur Clusters with Alternative Ligands. Model Studies Using Synthetic Analogues | Marie Bergner | Taschenbuch | 198 S. | Englisch | 2017 | Cuvillier | EAN 9783736996724 | Verantwortliche Person für die EU: Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen, info[at]cuvillier[dot]de | Anbieter: preigu Print on Demand. Seller Inventory # 110820688