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

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

Arizona State University

Research output: Contribution to journal › Article › peer-review

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

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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

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.",

author = "Nieman, {Ronald A.} and Devens Gust and Cronin, {John R.}",

note = "Funding Information: Support for this work was provided by the American Heart Association, Arizona Affiliate, and by the National Institutes of Health (GM 27200).",

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T1 - N-[1-13C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies

T2 - Acetylation of cytochrome c

AU - Nieman, Ronald A.

AU - Gust, Devens

AU - Cronin, John R.

N1 - Funding Information: Support for this work was provided by the American Heart Association, Arizona Affiliate, and by the National Institutes of Health (GM 27200).

PY - 1982/3/1

Y1 - 1982/3/1

N2 - 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.

AB - 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.

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