《Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases》 was published in Inorganic Chemistry in 2020. These research results belong to Miller, Kelsey R.; Paretsky, Jonathan D.; Follmer, Alec H.; Heinisch, Tillmann; Mittra, Kaustuv; Gul, Sheraz; Kim, In-Sik; Fuller, Franklin D.; Batyuk, Alexander; Sutherlin, Kyle D.; Brewster, Aaron S.; Bhowmick, Asmit; Sauter, Nicholas K.; Kern, Jan; Yano, Junko; Green, Michael T.; Ward, Thomas R.; Borovik, A. S.. Name: Bis(pyridin-2-ylmethyl)amine The article mentions the following:
An important class of non-heme dioxygenases contains a conserved Fe binding site that consists of a 2-His-1-carboxylate facial triad. Results from structural biol. show that, in the resting state, these proteins are six-coordinate with aqua ligands occupying the remaining three coordination sites. We have utilized biotin-streptavidin (Sav) technol. to design new artificial Fe proteins (ArMs) that have many of the same structural features found within active sites of these non-heme dioxygenases. An Sav variant was isolated that contains the S112E mutation, which installed a carboxylate side chain in the appropriate position to bind to a synthetic FeII complex confined within Sav. Structural studies using X-ray diffraction (XRD) methods revealed a facial triad binding site that is composed of two N donors from the biotinylated ligand and the monodentate coordination of the carboxylate from S112E. Two aqua ligands complete the primary coordination sphere of the FeII center with both involved in hydrogen bond networks within Sav. The corresponding FeIII protein was also prepared and structurally characterized to show a six-coordinate complex with two exogenous acetato ligands. The FeIII protein was further shown to bind an exogenous azido ligand through replacement of one acetato ligand. Spectroscopic studies of the ArMs in solution support the results found by XRD. Biol. O2 activation is often accomplished with dioxygenases that contain non-heme iron centers with a common 2-His-1-carboxylate endogenous binding site for iron. We have engineered an artificial protein to model this site using biotin-streptavidin technol. Structural and spectroscopic studies support formation of an Fe(II) artificial protein with features similar to those in the native proteins, including hydrogen bonds within the secondary coordination sphere. This work highlights the utility of embedding metal complexes with protein hosts.Bis(pyridin-2-ylmethyl)amine(cas: 1539-42-0Name: Bis(pyridin-2-ylmethyl)amine) was used in this study.
Bis(pyridin-2-ylmethyl)amine(cas: 1539-42-0) is a secondary amine with two picolyl substituents. As a tridentate ligand this compound provides three nitrogen donors that affords good selectivity for Zn2+ over biologically relevant metals such as Na+, K+, Mg2+ and Ca2+, and leaves coordination sites free for anion binding. Name: Bis(pyridin-2-ylmethyl)amine