L. Alfonta, Zhiwen Zhang, S. Uryu
Nov 6, 2003
Citations
4
Influential Citations
109
Citations
Quality indicators
Journal
Journal of the American Chemical Society
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.