Multinuclear Pyrazolate Based Copper Complexes by Konstanzer Vera (8 results)

PAP. Condition: New. New Book. Shipped from UK. Established seller since 2000.

Condition: New.

PAP. Condition: New. New Book. Shipped from UK. Established seller since 2000.

Taschenbuch. Condition: Neu. This item is printed on demand - it takes 3-4 days longer - Neuware -Enzymes with multicopper active sites play important roles in many biological processes. Recently a novel multinuclear copper site was discovered in N2O-Reductase and its exact structure and mechanism has been much discussed since then. The so called CuZ center contains a unique tetranuclear Cu4S2-Cluster, which is coordinated by seven histidine residues. Until now no synthetic model complex could be isolated that emulates the Cu4S2 core of the active site.In this thesis a new strategy towards such model systems is introduced. To mimic the nitrogen-rich environment of the copper ions, pyrazolate-based ligand scaffolds with chelating N-donor side arms are employed. The resulting binuclear metal complexes were isolated and fully characterized. Additionally the reactivity of these binuclear building blocks towards various sulfur-containing coligands and sulfur-transfer reagents was investigated. 206 pp. Englisch.…

Condition: New. Dieser Artikel ist ein Print on Demand Artikel und wird nach Ihrer Bestellung fuer Sie gedruckt. KlappentextrnrnEnzymes with multicopper active sites play important roles in many biological processes. Recently a novel multinuclear copper site was discovered in N2O-Reductase and its exact structure and mechanism has been much discussed since.…

Taschenbuch. Condition: Neu. This item is printed on demand - Print on Demand Titel. Neuware -Enzymes with multicopper active sites play important roles in many biological processes. Recently a novel multinuclear copper site was discovered in N2O-Reductase and its exact structure and mechanism has been much discussed since then. The so called CuZ center contains a unique tetranuclear Cu4S2-Cluster, which is coordinated by seven histidine residues. Until now no synthetic model complex could be isolated that emulates the Cu4S2 core of the active site.In this thesis a new strategy towards such model systems is introduced. To mimic the nitrogen-rich environment of the copper ions, pyrazolate-based ligand scaffolds with chelating N-donor side arms are employed. The resulting binuclear metal complexes were isolated and fully characterized. Additionally the reactivity of these binuclear building blocks towards various sulfur-containing coligands and sulfur-transfer reagents was investigated.Cuvillier Verlag, Nonnenstieg 8, 37075 Göttingen 206 pp. Englisch.…

Taschenbuch. Condition: Neu. nach der Bestellung gedruckt Neuware - Printed after ordering - Enzymes with multicopper active sites play important roles in many biological processes. Recently a novel multinuclear copper site was discovered in N2O-Reductase and its exact structure and mechanism has been much discussed since then. The so called CuZ center contains a unique tetranuclear Cu4S2-Cluster, which is coordinated by seven histidine residues. Until now no synthetic model complex could be isolated that emulates the Cu4S2 core of the active site.In this thesis a new strategy towards such model systems is introduced. To mimic the nitrogen-rich environment of the copper ions, pyrazolate-based ligand scaffolds with chelating N-donor side arms are employed. The resulting binuclear metal complexes were isolated and fully characterized. Additionally the reactivity of these binuclear building blocks towards various sulfur-containing coligands and sulfur-transfer reagents was investigated.…

Taschenbuch. Condition: Neu. Multinuclear Pyrazolate-Based Copper Complexes Inspired by the CuZ-Site of N2O-Reductases | Vera Konstanzer | Taschenbuch | Kartoniert / Broschiert | Englisch | 2011 | Cuvillier | EAN 9783869559780 | Verantwortliche Person für die EU: preigu GmbH & Co. KG, Lengericher Landstr. 19, 49078 Osnabrück, mail[at]preigu[dot]de | Anbieter: preigu Print on Demand.…