Dioxygen Reactivity of Fully Reduced [LFeII···CuI]+ Complexes Utilizing Tethered Tetraarylporphyrinates: Active Site Models for Heme-Copper Oxidases
Inorganic Chemistry1999Vol. 38(10), pp. 2244–2245
Citations Over TimeTop 16% of 1999 papers
Telvin D. Ju, Reza A. Ghiladi, Dong-Heon Lee, Gino P. F. van Strijdonck, Amina S. Woods, Robert J. Cotter, Victor G. Young, Kenneth D. Karlin
Abstract
For O2-reactivity studies aimed at modeling aspects of heme-copper oxidase enzyme function, use of heterobinucleating ligands (6-pyridyl (6L) or 5-pyridyl (5L) connection) gives rise to iron(II) (with “empty-tether”), 2a and 2b, and [LFeII···CuI]+ complexes, 3a and 3b, respectively. Reduced complexes 2 and 3 can exist in high-, intermediate-, or low-spin iron(II) configurations, depending on the solvent employed. Reaction of dioxygen with both 3a and 3b leads to a biomimetic reductive O−O bond cleavage forming μ-oxo species [(L)FeIII−O−CuII]+ (4a, 4b). The X-ray structure of 4a is reported.
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