Details

Autor(en) / Beteiligte

• van der Vlugt, Jarl Ivar
• Meyer, Franc
• Sigel, Roland K. O
• Sigel, Helmut
• Sigel, Astrid

Titel

Synthetic Models for the Active Sites of Nickel‐Containing Enzymes

Ist Teil von

• Nickel and Its Surprising Impact in Nature, 2007, p.181-239

Ort / Verlag

Chichester, UK: John Wiley & Sons, Ltd

Erscheinungsjahr

2007

Link zum Volltext

Quelle

Wiley Online Library All Obooks

Beschreibungen/Notizen

• Small‐molecule synthetic model complexes are of great importance for the understanding of native metalloenzyme active sites for a variety of reasons. Insight into spectroscopic and structural features of the natural system can be provided by characterization and investigation of simplified, isolable synthetic analogues. Furthermore, significant progress can be made towards unraveling possible reaction mechanisms and pathways by studying functional model systems. Finally, the enzyme active sites may be viewed as valuable blueprints for the development of novel bioinspired catalysts for synthetically useful substrate transformations. This chapter focuses on small‐molecule synthetic model complexes for six different nickel‐containing metalloenzyme active sites, i.e., cofactor F 430 , nickel‐iron hydrogenase, acetyl coenzyme A synthase/CO dehydrogenase, superoxide dismutase, urease, and acireductone reductase. Focus for each type of active site is put on recent breakthroughs, with descriptions of both structural and functional models, together with a relation to key features observed for the natural system involved. It is meant to introduce the reader to the approaches available to and used by the inorganic/coordination chemist in contributing to nowadays problems and challenges in bioinorganic nickel chemistry.