69519-27-3Relevant academic research and scientific papers
Deciphering the mechanism of O2 reduction with electronically tunable non-heme iron enzyme model complexes
Surendhran, Roshaan,D'Arpino, Alexander A.,Sciscent, Bao Y.,Cannella, Anthony F.,Friedman, Alan E.,MacMillan, Samantha N.,Gupta, Rupal,Lacy, David C.
, p. 5773 - 5780 (2018/07/13)
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.
