Nature contains metalloproteins that can perform a variety of different functions, such as electron transfer or the activation of small molecules (e. g. O2, H2, CO2). The reactivity of immobilized metallocofactors are regulated by several components that includes the type of transition metal ion, the donor set that defines the primary coordination sphere, and structure of the second coordination sphere. Of these components, the effects of the secondary coordination sphere are least understood and there is a need to develop approaches to probe its influence on the function of metal ions. We are working on an approach that utilizes biotin-streptavidin technology to immobilize biologically relevant metal complexes within a protein host. Streptavidin (Sav) is a homotetramer that assembles as a dimer of dimers and is stable over a broad range of temperature and pH. Each dimer is arranged such that the biotin-binding sites face each other, which creates a volume of space to immobilize metal complexes. We are investigated methods for positioning biotinylated metal complexes within the dimers to promote both mononuclear and dinuclear complexes. This presentation will highlight our efforts in producing both types of "active sites" for a series of biotinylated Cu complexes. The structures, physical, and reactivity properties of the new artificial Cu proteins will be discussed.

Immobilization of synthetic Cu complexes within a protein host

255th National Meeting (2018)

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