Artificial Iron Proteins: Modeling the Active Sites in Non-Heme Dioxygenases.

ABSTRACT: 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 biology 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) technology 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 Fe^II complex confined within Sav. Structural studies using X-ray diffraction (XRD) methods revealed a facial triad bindi

SUBMITTER: Miller KR 

PROVIDER: S-EPMC7219546 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature