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Issue 26, 2018
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Deciphering the mechanism of O2 reduction with electronically tunable non-heme iron enzyme model complexes

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Abstract

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.

Graphical abstract: Deciphering the mechanism of O2 reduction with electronically tunable non-heme iron enzyme model complexes

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Publication details

The article was received on 10 Apr 2018, accepted on 04 Jun 2018 and first published on 05 Jun 2018


Article type: Edge Article
DOI: 10.1039/C8SC01621F
Citation: Chem. Sci., 2018,9, 5773-5780
  • Open access: Creative Commons BY-NC license
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    Deciphering the mechanism of O2 reduction with electronically tunable non-heme iron enzyme model complexes

    R. Surendhran, A. A. D'Arpino, B. Y. Sciscent, A. F. Cannella, A. E. Friedman, S. N. MacMillan, R. Gupta and D. C. Lacy, Chem. Sci., 2018, 9, 5773
    DOI: 10.1039/C8SC01621F

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