Deciphering the mechanism of O2 reduction with electronically tunable non-heme iron enzyme model complexes
| Autor: | Rupal Gupta, Alexander A D'Arpino, Bao Y Sciscent, Roshaan Surendhran, Anthony F. Cannella, Alan E. Friedman, Samantha N. MacMillan, David C. Lacy |
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| Rok vydání: | 2018 |
| Předmět: |
010405 organic chemistry
Chemistry General Chemistry Rate equation Crystal structure 010402 general chemistry 01 natural sciences 0104 chemical sciences 3. Good health Reduction (complexity) Homologous series chemistry.chemical_compound Crystallography Hammett equation Enzyme model Non heme iron Structural motif |
| Zdroj: | Chemical Science. 9:5773-5780 |
| ISSN: | 2041-6539 2041-6520 |
| DOI: | 10.1039/c8sc01621f |
| Popis: | A homologous series of electronically tuned 2,2',2''-nitrilotris(N-arylacetamide) pre-ligands (H3LR ) were prepared (R = NO2, CN, CF3, F, Cl, Br, Et, Me, H, OMe, NMe2) and some of their corresponding Fe and Zn species synthesized. The iron complexes react rapidly with O2, the final products of which are diferric mu-oxo bridged species. The crystal structure of the oxidized product obtained from DMA solutions contain a structural motif found in some diiron proteins. The mechanism of iron mediated O2 reduction was explored to the extent that allowed us to construct an empirically consistent rate law. A Hammett plot was constructed that enabled insightful information into the rate-determining step and hence allows for a differentiation between two kinetically equivalent O2 reduction mechanisms. |
| Databáze: | OpenAIRE |
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