Dinitrosyl Iron Complexes Relevant to Rieske Cluster Nitrosylation

摘要

Iron-sulfur clusters are among the most ubiquitous cofactors in biology. The diversity of structures encountered in iron-sulfur proteins reflects the many functions nature employs for these versatile units, from electron transfer to substrate binding and activation. Of the many variations of iron-sulfur clusters, only a select few have ligands other than cysteine. Among these, the best-documented examples are Rieske-type Fe_2S_2 clusters that contain a pair of histidine residues ligating one iron atom. Recently, the first synthetic analogue of a Rieske cluster was reported (1, Scheme 1). We were interested to explore the nitric oxide reactivity of such a compound as part of ongoing investigations into the reactivity of non-heme iron with NO.