A Nickel(II)-Containing Vitamin B12Derivative with a Cofactor-F430-type π-System
| Autor: | Christopher Brenig, René M. Oetterli, Felix Zelder, Lucas Prieto |
|---|---|
| Rok vydání: | 2018 |
| Předmět: |
Cofactor F430
biology 010405 organic chemistry Ligand Stereochemistry Corrin Active site General Chemistry 010402 general chemistry 01 natural sciences Catalysis 0104 chemical sciences chemistry.chemical_compound Corrinoid chemistry Cobaltocene biology.protein Anaerobic bacteria Derivative (chemistry) |
| Zdroj: | Angewandte Chemie International Edition. 57:16308-16312 |
| ISSN: | 1433-7851 |
| DOI: | 10.1002/anie.201810983 |
| Popis: | F430 is a unique enzymatic cofactor in the production and oxidation of methane by strictly anaerobic bacteria. The key enzyme methyl coenzyme M reductase (MCR) contains a hydroporphinoid nickel complex with a characteristic absorption maximum at around 430 nm in its active site. Herein, the three-step semisynthesis of a hybrid NiII -containing corrinoid that partly resembles F430 in its structural and spectroscopic features from vitamin B12 is presented. A key step of the route is the simultaneous demetalation and ring closure reaction of a 5,6-secocobalamin to metal-free 5,6-dihydroxy-5,6-dihydrohydrogenobalamin with cobaltocene and KCN under reductive conditions. Studies on the coordination chemistry of the novel compound support an earlier hypothesis why nature carefully selected a corphin over a corrin ligand in F430 for challenging nickel-catalyzed biochemical reactions. |
| Databáze: | OpenAIRE |
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