NMR and Mossbauer Studies Reveal a Temperature-Dependent Switch from S = 1 to 2 in a Nonheme Oxoiron(IV) Complex with Faster C-H Bond Cleavage Rates.

ABSTRACT: S = 2 Fe^IV═O centers generated in the active sites of nonheme iron oxygenases cleave substrate C-H bonds at rates significantly faster than most known synthetic Fe^IV═O complexes. Unlike the majority of the latter, which are S = 1 complexes, [Fe^IV(O)(tris(2-quinolylmethyl)amine)(MeCN)]²⁺ (3) is a rare example of a synthetic S = 2 Fe^IV═O complex that cleaves C-H bonds 1000-fold faster than the related [Fe^IV(O)(tris(pyridyl-2-methyl)amine)(MeCN)]²⁺ complex (0). To rationalize this significant difference, a systematic comparison of properties has been carried out on 0 and 3 as well as related complexes 1 and 2 with mixed pyridine (Py)/quinoline (Q) ligatio

SUBMITTER: Rasheed W 

PROVIDER: S-EPMC11238627 | biostudies-literature | 2024 Feb

REPOSITORIES: biostudies-literature