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

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

doi:10.1021/ja038242x

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 journal › Article › peer-review

121 Scopus citations

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.

Original language	English
Pages (from-to)	14662-14663
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	125
Issue number	48
DOIs	https://doi.org/10.1021/ja038242x
State	Published - 3 Dec 2003
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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10.1021/ja038242x

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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.",

author = "Lital Alfonta and Zhiwen Zhang and Sean Uryu and Loo, {Joseph A.} and Schultz, {Peter G.}",

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AU - Alfonta, Lital

AU - Zhang, Zhiwen

AU - Uryu, Sean

AU - Loo, Joseph A.

AU - Schultz, Peter G.

PY - 2003/12/3

Y1 - 2003/12/3

N2 - 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.

AB - 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.

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JO - Journal of the American Chemical Society

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ER -

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

Abstract

ASJC Scopus subject areas

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