N-[1-13C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies: Acetylation of cytochrome c

Ronald A. Nieman; John Devens Gust; John R. Cronin

doi:10.1016/0003-2697(82)90356-6

N-[1-¹³C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies: Acetylation of cytochrome c

Ronald A. Nieman, John Devens Gust, John R. Cronin

Arizona State University

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2 Citations (Scopus)

Abstract

The reaction of N-[1-¹³C] acetylimidazole with cytochrome c and guanidinated cytochrome c was evaluated as a means of introducing NMR-detectable groups as conformation-dependent probes. Resonances from both N-[1-¹³C]acetyl lysyl and O-[1-¹³C]acetyl tyrosyl groups were observed when ferricytochrome c was acetylated. However, only O-[1-¹³C]acetyl tyrosyl resonances were seen with acetylated guanidinated ferricytochrome c. Chemical shifts of the four O-[1-¹³C]acetyl tyrosyl groups were conformation dependent and ranged from 172 to 176 ppm. A convenient method for the preparation of N-[1-¹³C]acetylimidazole is described.

Original language	English
Pages (from-to)	347-350
Number of pages	4
Journal	Analytical Biochemistry
Volume	120
Issue number	2
DOIs	https://doi.org/10.1016/0003-2697(82)90356-6
Publication status	Published - Mar 1 1982

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ASJC Scopus subject areas

Biochemistry
Biophysics
Molecular Biology

Cite this

Nieman, R. A., Gust, J. D., & Cronin, J. R. (1982). N-[1-¹³C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies: Acetylation of cytochrome c. Analytical Biochemistry, 120(2), 347-350. https://doi.org/10.1016/0003-2697(82)90356-6

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10.1016/0003-2697(82)90356-6