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

Research output: Contribution to journal › Article

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

Fingerprint

Acetylation

Cytochromes c

Nuclear magnetic resonance

Conformations

Proteins

Chemical shift

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

N-[1-¹³C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies : Acetylation of cytochrome c. / Nieman, Ronald A.; Gust, John Devens; Cronin, John R.

In: Analytical Biochemistry, Vol. 120, No. 2, 01.03.1982, p. 347-350.

Research output: Contribution to journal › Article

Nieman, RA, Gust, JD & Cronin, JR 1982, 'N-[1-¹³C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies: Acetylation of cytochrome c', Analytical Biochemistry, vol. 120, no. 2, pp. 347-350. https://doi.org/10.1016/0003-2697(82)90356-6

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

Nieman, Ronald A. ; Gust, John Devens ; Cronin, John R. / N-[1-¹³C]acetylimidazole as a reagent for tyrosyl modification in protein NMR studies : Acetylation of cytochrome c. In: Analytical Biochemistry. 1982 ; Vol. 120, No. 2. pp. 347-350.

@article{9537b5244cd84bbea0c40adc52ab1c09,

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 Gust, {John Devens} and Cronin, {John R.}",

year = "1982",

month = "3",

day = "1",

doi = "10.1016/0003-2697(82)90356-6",

language = "English",

volume = "120",

pages = "347--350",

journal = "Analytical Biochemistry",

issn = "0003-2697",

publisher = "Academic Press Inc.",

number = "2",

}

TY - JOUR

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, John Devens

AU - Cronin, John R.

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.

UR - http://www.scopus.com/inward/record.url?scp=0020110690&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020110690&partnerID=8YFLogxK

U2 - 10.1016/0003-2697(82)90356-6

DO - 10.1016/0003-2697(82)90356-6

M3 - Article

C2 - 6283939

AN - SCOPUS:0020110690

VL - 120

SP - 347

EP - 350

JO - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

IS - 2

ER -

Access to Document

10.1016/0003-2697(82)90356-6