Abstract
Redox active amino acids, cofactors, and metal ions are involved in a large number of catalytic, electron transfer, and regulatory processes in biology. Consequently, the ability to engineer redox active centers at defined sites in proteins would facilitate both the study and manipulation of a wide range of biological processes. Recently, we demonstrated that the redox active amino acid 3,4-dihydroxyphenylalanine could be efficiently and selectively incorporated into proteins in Escherichia coli using a nonsense codon and a corresponding orthogonal tRNA/aminoacyl-tRNA synthetase pair. We now report that ferrocene derivative 1 can be genetically encoded in Saccharomyces cerevisiae ( S. cerevisiae) in good yield in response to the amber codon, TAG.
Published Version
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