STRUCTURAL CHARACTERIZATION OF HEME PROTEINS MINERALIZED WITHIN THE ZIF-8 METAL ORGANIC FRAMEWORK

Dylan Grassie and Randy W. Larsen*

Department of Chemistry, Univesrity of South Florida, Tampa, FL 33620

The ability to encapsulate bioactive molecules and enzymes within porous solid state materials has long been of interest in the development of hybrid materials for industrial applications. Metal organic frameworks (MOFs) are of particular interest for encapsulation of these molecules for their regularly porous cavities of tunable dimensions, ease of synthesis, and functionalizable interiors. Recently the ability to mineralize various proteins within several zeolitic imidazole frameworks (ZIFs) has been demonstrated in which the MOF grows around the protein creating large protein encapsulated cavities. These materials have been shown to have unique catalytic activity which is promising for industrial reactions. The most widely investigated material is ZIF-8 formed from Zn(II) ions and 2-methyl imidazole. Here we report protein structural studies to determine the impact of mineralization on the proteins three dimensional structure. For this study myoglobin (Mb), cytochrome c (Cc), and Microperoxidase-11 (MP-11) have been selected as targets for mineralization in ZIF-8.