De novo biosynthesis of a nonnatural cobalt porphyrin cofactor inE. coliand incorporation into hemoproteins

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Abstract
Significance: Enzymes rely on cofactors, both organic molecules and metal ions, for reactivity beyond what can be performed with the 20 standard amino acids. One way to expand the reactivity of heme-dependent proteins is to swap the native iron atom in the heme cofactor for a different metal. Because the resulting metal-containing cofactor is new to nature, methods for producing these nonnative hemoproteins are difficult and often limited to the test tube. Here, we report a method for subverting the heme biosynthetic pathway inE. colito produce cobalt protoporphyrin IX (CoPPIX) and CoPPIX-substituted hemoproteins in living cells. This method enables the use of CoPPIX-substituted enzymes as biocatalysts and widens the scope of proteins that may be studied by metal substitution.
Funding Information
  • National Science Foundation (DGE-1747503)

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