Spectroscopic and metal binding properties of a de novo metalloprotein binding a tetrazinc cluster.

ABSTRACT: De novo design provides an attractive approach, which allows one to test and refine the principles guiding metalloproteins in defining the geometry and reactivity of their metal ion cofactors. Although impressive progress has been made in designing proteins that bind transition metal ions including iron-sulfur clusters, the design of tetranuclear clusters with oxygen-rich environments remains in its infancy. In previous work, we described the design of homotetrameric four-helix bundles that bind tetra-Zn²⁺ clusters. The crystal structures of the helical proteins were in good agreement with the overall design, and the metal-binding and conformational properties of the helical bundles in solution were consistent with the crystal structures. However, the corresponding apo-proteins

SUBMITTER: Chino M 

PROVIDER: S-EPMC6218314 | biostudies-literature | 2018 Aug

REPOSITORIES: biostudies-literature