TY - JOUR
T1 - Ribosyl-diphthamide
T2 - Confirmation of structure by fast atom bombardment mass spectrometry
AU - Bodley, James W.
AU - Upham, Roger
AU - Crow, Frank W.
AU - Tomer, Kenneth B.
AU - Gross, Michael L.
N1 - Funding Information:
1 This work was supported by National Institutes of Health Grant GM-26332 to J. W. B. and by the Midwest Center for Maas Spectrometry, a National Science Foundation Regional Instrumentation Facility (Grant CHE 82-3211164). This is a paper XXX1 in the series “Studies on Translocation”. The preceding paper in the series is Ref. (1). a To whom correspondence should be addressed.
PY - 1984/5/1
Y1 - 1984/5/1
N2 - Diphtheria toxin inactivates protein synthesis elongation factor 2 by attaching ADP-ribose to an unusual post-translational amino acid derivative, diphthamide, in the factor. Previously, we prepared ribosyl-diphthamide from the ADP-ribosyl-factor and proposed on the basis of NMR spectral analysis that it is 1-α-d-ribofuranosyl-2-[3-carboxyamido-3-(trimethylammonio)propyl]histidine [N. J. Oppenheimer, and J. W. Bodley, (1981) J. Biol. Chem. 256, 8579-8581 and op. cit.]. Now, using fast atom bomardment mass spectrometry, the intact cation of ribosyl-diphthamide has been observed in the gas phase. The theoretical mass of the structure proposed for ribosyl-diphthamide uniquely agrees with the observed mass of the inact cation of the compound to within 2 ppm. Collisional activation decomposition mass spectral analysis provided additional structural confirmation. Thus, although the compound has not been synthesized, all available evidence appears uniquely consistent with the structure of ribosyl-diphthamide previously proposed.
AB - Diphtheria toxin inactivates protein synthesis elongation factor 2 by attaching ADP-ribose to an unusual post-translational amino acid derivative, diphthamide, in the factor. Previously, we prepared ribosyl-diphthamide from the ADP-ribosyl-factor and proposed on the basis of NMR spectral analysis that it is 1-α-d-ribofuranosyl-2-[3-carboxyamido-3-(trimethylammonio)propyl]histidine [N. J. Oppenheimer, and J. W. Bodley, (1981) J. Biol. Chem. 256, 8579-8581 and op. cit.]. Now, using fast atom bomardment mass spectrometry, the intact cation of ribosyl-diphthamide has been observed in the gas phase. The theoretical mass of the structure proposed for ribosyl-diphthamide uniquely agrees with the observed mass of the inact cation of the compound to within 2 ppm. Collisional activation decomposition mass spectral analysis provided additional structural confirmation. Thus, although the compound has not been synthesized, all available evidence appears uniquely consistent with the structure of ribosyl-diphthamide previously proposed.
UR - http://www.scopus.com/inward/record.url?scp=0021436591&partnerID=8YFLogxK
U2 - 10.1016/0003-9861(84)90439-9
DO - 10.1016/0003-9861(84)90439-9
M3 - Article
C2 - 6712255
AN - SCOPUS:0021436591
SN - 0003-9861
VL - 230
SP - 590
EP - 593
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -