The synthesis and spectroscopic characterization of [Fe(NO)(N3PyS)]BF4 (3) is presented, the first structural and electronic model of NO-bound cysteine dioxygenase (CDO). The nearly isostructural all-N-donor analog [Fe(NO)(N4Py)](BF4)2 (4) was also prepared, and comparisons of 3 and 4 provide insight regarding the influence of S versus N ligation in {FeNO}7 species. One key difference occurs upon photoirradiation, which causes the fully reversible release of NO from 3, but not from 4.
The non-heme iron enzyme cysteine dioxygenase (CDO) catalyzes the S-oxygenation of cysteine by O2 to cysteine sulfinic acid. The synthesis of a new structural and functional model of the cysteine-bound CDO active site, [FeII(N3PyS)(CH3CN)]BF4 (1) is reported. This complex is prepared with a new facially chelating 4N/1S(thiolate) pentadentate ligand. Reaction of 1 with O2 results in oxygenation of the thiolate donor to afford the doubly-oxygenated sulfinate product [FeII(N3PySO2)(NCS)] (2), which was crystallographically characterized. The thiolate donor provided by the new N3PyS ligand has a dramatic influence on the redox potential and O2 reactivity of this iron(II) model complex.
One-electron reduction of [Fe(NO)-(N3PyS)]BF4 (1) leads to the production of the metastable nonheme {FeNO}8 complex, [Fe(NO)(N3PyS)] (3). Complex 3 is a rare example of a high-spin (S = 1) {FeNO}8, and is the first example, to our knowledge, of a mononuclear nonheme {FeNO}8 species that generates N2O. A second, novel route to 3 involves addition of Piloty’s acid, an HNO donor, to an FeII precursor. This work provides possible new insights regarding the mechanism of nitric oxide reductases.
The S-oxygenation of cysteine with dioxygen to give cysteine sulfinic acid occurs at the non-heme iron active site of cysteine dioxygenase. Similar S-oxygenation events occur in other non-heme iron enzymes, including nitrile hydratase and isopenicillin N synthase, and these enzymes have inspired the development of a class of [NxSy]-Fe model complexes. Certain members of this class have provided some intriguing examples of S-oxygenation, and this article summarizes these results, focusing on the non-heme iron(II/III)-thiolate model complexes that are known to react with O2 or in some cases other O-atom transfer oxidants, to yield sulfur oxygenates. Key aspects of the synthesis, structure, and reactivity of these systems are presented, along with any mechanistic information available on the oxygenation reactions. A number of iron(III)-thiolate complexes react with O2 to give S-oxygenates, and the degree to which the thiolate sulfur donors are oxidized varies among the different complexes, depending upon the nature of the ligand, metal geometry, and spin state. The first examples of iron(II)-thiolate complexes that react with O2 to give selective S-oxygenation are just emerging. Mechanistic information on these transformations is limited, with isotope labeling studies providing much of the current mechanistic data. The many questions that remain unanswered for both models and enzymes provide strong motivation for future work in this area.
The non-heme iron complexes, [FeII(N3PySR)(CH3CN)](BF4)2 (1) and [FeII(N3PyamideSR)](BF4)2 (2), afford rare examples of metastable Fe(iii)-OOH and Fe(iii)-OOtBu complexes containing equatorial thioether ligands and a single H-bond donor in the second coordination sphere. These peroxo complexes were characterized by a range of spectroscopic methods and density functional theory studies. The influence of a thioether ligand and of one H-bond donor on the stability and spectroscopic properties of these complexes was investigated.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.