DFsc is a monomeric de novo designed protein created to model naturally occurring di-iron carboxylate enzymes.  Rubrerythrin is a naturally occurring di-iron protein that exhibits peroxidase activity.  The active site of rubrerythrin differs from the DFsc model protein by the presence of one extra carboxylate residue.  We have inserted an additional carboxylate residue (Glu or Asp) at position 14 in the amino acid sequence of DFsc with the goal of altering it from a phenol oxidase to a peroxidase that can be used as a rubrerythin model.  The proteins were analyzed for composition and characterized for secondary structure, metal binding ability, and ferroxidase activity.  Our results show that both proteins bind to a variety of divalent metal ions, are well folded in the absence and presence of metal ions at neutral pH, and exhibit an absorption feature near 350 nm upon addition of Fe2+ characteristic of the activation of dioxygen.

Di-iron proteins: Formation of a rubrerythrin (Rbr) replica protein from a DFsc model protein

243rd National Meeting (2012)

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