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.
Site-specific incorporation of a redox-active amino acid into proteins. Publishing Authors By Initials
Site-specific incorporation of a redox-active amino acid into proteins. Journal Published:
PUBLICATION TYPE: Research Support, U.S. Gov't,
Journal: Journal of the American Chemical Society
VOLUME: 125
Page Numbers: 14662-3
Journal Abbreviation: J. Am. Chem. Soc.
ISSN: 0002-7863
DAY: 3
MONTH: Dec
YEAR: 2003
Site-specific incorporation of a redox-active amino acid into proteins. Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 7503056
Site-specific incorporation of a redox-active amino acid into proteins. Keywords Mesh Terms:
KEYWORDS: Whales
MESH TERMS: metabolism
Chemical & Substance for Abstract: Site-specific incorporation of a redox-active amino acid into proteins. Information
Substance Name: Amino Acyl-tRNA Synthetases
Registry Number: EC 6.1.1.-
Grant and Affiliation Information for Site-specific incorporation of a redox-active amino acid into proteins.
AFFILIATION: Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.
Country: United States
AGENCY: United States NIGMS
GRANT: GM 66494
ACRONYM: GM
MEDLINETA: J Am Chem Soc
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