A Binuclear Cu_A Center Designed in an All α-Helical Protein Scaffold.

ABSTRACT: The primary and secondary coordination spheres of metal binding sites in metalloproteins have been investigated extensively, leading to the creation of high-performing functional metalloproteins; however, the impact of the overall structure of the protein scaffold on the unique properties of metalloproteins has rarely been studied. A primary example is the binuclear Cu_A center, an electron transfer cupredoxin domain of photosynthetic and respiratory complexes and, recently, a protein coregulated with particulate methane and ammonia monooxygenases. The redox potential, Cu-Cu spectroscopic features, and a valence delocalized state of Cu_A are difficult to reproduce in synthetic models, and every artificial protein Cu_A center to-date has used a modified cupredo

SUBMITTER: Mirts EN 

PROVIDER: S-EPMC8168375 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature