Metal-binding sites in metalloproteins frequently occur at the interfaces of elements of secondary structure, which has enabled the retrostructural analysis of natural proteins and the de novo design of helical bundles that bind metal ion cofactors. However, the design of metalloproteins containing β-structure is less well developed, despite the frequent occurrence of β-conformations in natural metalloproteins. Here, we describe the design and construction of a β-protein, RM1, that forms a stable, redox-active 4-Cys thiolate Fe(II/III) site analogous to the active site of rubredoxin. The protein folds into a β-structure in the presence and absence of metal ions and binds Fe(II/III) to form a redox-active site that is stable to repeated cycles of oxidation and reduction, even in an aerobic environment.
|Original language||English (US)|
|Number of pages||2|
|Journal||Journal of the American Chemical Society|
|State||Published - Apr 27 2005|
All Science Journal Classification (ASJC) codes
- Colloid and Surface Chemistry