Site-Specific Incorporation of a Redox-Active Amino Acid into Proteins

Lital Alfonta, Zhiwen Zhang, Sean Uryu, Joseph A. Loo, Peter G. Schultz

Research output: Contribution to journalArticlepeer-review

113 Scopus citations


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.

Original languageEnglish
Pages (from-to)14662-14663
Number of pages2
JournalJournal of the American Chemical Society
Issue number48
StatePublished - 3 Dec 2003
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


Dive into the research topics of 'Site-Specific Incorporation of a Redox-Active Amino Acid into Proteins'. Together they form a unique fingerprint.

Cite this