Abstract
A series of NO-bound, iron-functionalized polyoxovanadate-alkoxide (FePOV-alkoxide) clusters have been synthesized, providing insight into the role of multimetallic constructs in the coordination and activation of a substrate. Upon exposure of the heterometallic cluster to NO, the vanadium-oxide metalloligand is oxidized by a single electron, shuttling the reducing equivalent to the {FeNO} subunit to form a {FeNO}7 species. Four NO-bound clusters with electronic distributions ranging from [VV3VIV2]{FeNO}7 to [VIV5]{FeNO}7 have been synthesized, and characterized via 1H NMR, infrared, and electronic absorption spectroscopies. The ability of the FePOV-alkoxide cluster to store reducing equivalents in the metalloligand for substrate coordination and activation highlights the ultility of the metal-oxide scaffold as a redox reservoir.
Highlights
The chemical reactivity of nitric oxide (NO) has captivated the eld of bioinorganic chemistry, due to the participation of this small molecule in vasodilation, mammalian signalling, and immune defence processes.[1]
Using a suite of analytical techniques, we have demonstrated that the metal-oxide metalloligand functions as a redox reservoir for the ferric centre, storing reducing equivalents across the vanadyl ions in a delocalized cloud of electron density
To investigate the reactivity of NO with high-spin ferric centres embedded within a multimetallic cluster, NO(g) was added to a solution of the neutral, FePOV–alkoxide cluster, [VI4VVVO6(OCH3)12FeIII] (1-V5Fe) (Scheme 1)
Summary
The chemical reactivity of nitric oxide (NO) has captivated the eld of bioinorganic chemistry, due to the participation of this small molecule in vasodilation, mammalian signalling, and immune defence processes.[1]. The prevalence of heme- and non-heme-containing metalloenzymes in NO reductases has driven interest in understanding the electronic structure of the {FeNO} subunit in metalloproteins and model complexes.[6,7,8] A combination of spectroscopic, crystallographic, and theoretical methods have shown that substrate binding and reduction are key steps in NO activation.[2,3,9,10,11,12,13] despite reports describing the behaviour of NO with ferric and ferrous heme complexes, the chemistry of this substrate with non-heme derivatives remains underdeveloped (Fig. 1). Toward a more complete understanding of the redox chemistry involved during NO activation, the synthesis, characterization, and reactivity of non-heme models, capable of supporting variable oxidation states of the {FeNO} subunit, are of interest
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