Dinitrosyl iron complexes (DNICs) are inorganic compounds that have gained increasing attention in recent years due to the roles they play in biological systems. Biological DNICs can be low molecular weight or protein-bound and in both cases the most common ligands bound to the {Fe(NO)2}9 fragment are cysteine thiolates. The reactivity of oxygen with a series of biomimetic {Fe(NO2}9 DNICs bearing thiolate ligands has been investigated [1] will be described. These reactions result in the formation of the corresponding Roussin's red esters along with thiolate oxidation. This reactivity is contrasted with that previously reported for {Fe(NO)2-}10complexes [2]. The implications that this reactivity has for the as yet unidentified role of DNICs in the oxidative post-translational modification of proteins will be discussed.[1] J. Fitzpatrick, H. Kalyvas, J. Shearer, and E. Kim. 'Dioxygen mediated conversion of {Fe(NO)2}9 dinitrosyl iron complexes to Roussin's red esters.' Chem. Commun.  , 2013, 49 , 5550-5552.[2] K. M. Skodje, P. G. Williard, and E. Kim. 'Conversion of {Fe(NO)2}10 dinitrosyl iron to nitrato iron(III) species by molecular oxygen.' Dalton Trans.  , 2012, 41 , 7849-7851.

Novel reactivity of {Fe(NO)<sub>2</sub>}<sup>9</sup> dinitrosyl iron complexes and its implications in protein post-translational modification

247th National Meeting (2014)

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Novel reactivity of {Fe(NO)2}9 dinitrosyl iron complexes and its implications in protein post-translational modification

Novel reactivity of {Fe(NO)₂}⁹ dinitrosyl iron complexes and its implications in protein post-translational modification