Site-specific incorporation of a redox-active amino acid into proteins.
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.
Alfonta
Lital
L
Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Zhang
Zhiwen
Z
Uryu
Sean
S
Loo
Joseph A
JA
Schultz
Peter G
PG
D000604:Amino Acyl-tRNA Synthetases / Q000235:genetics / Q000378:metabolism; D000818:Animals; D003062:Codon; D004295:Dihydroxyphenylalanine / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D017017:Methanococcus / Q000201:enzymology / Q000235:genetics; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D010084:Oxidation-Reduction; D021241:Spectrometry, Mass, Electrospray Ionization; D014907:Whales
D003062:Codon; D009211:Myoglobin; D004295:Dihydroxyphenylalanine; D000604:Amino Acyl-tRNA Synthetases