Site-Specific incorporation of a Redox Active Amino Acid into Proteins. Academic Article uri icon

abstract

  • The redox-active amino acid 3, 4-dihydroxy-l-phenylalanine (DHP), which can undergo two-electron oxidation to a quinone, has been incorporated selectively and efficiently into proteins in Escherichia coli in response to a TAG codon. We have demonstrated that DHP can be oxidized electrochemically within the protein. The ability to incorporate a redox-active amino acid site specifically into proteins should facilitate the study of electron transfer in proteins, as well as enable the engineering of redox proteins with novel properties.

publication date

  • January 1, 2003