Premium
Probing sites of histidine phosphorylation with iodination and tandem mass spectrometry
Author(s) -
Sun Qingyu,
Julian Ryan R.
Publication year - 2011
Publication title -
rapid communications in mass spectrometry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.528
H-Index - 136
eISSN - 1097-0231
pISSN - 0951-4198
DOI - 10.1002/rcm.5116
Subject(s) - chemistry , histidine , phosphorylation , tandem mass spectrometry , mass spectrometry , lability , tandem , chromatography , proteomics , biochemistry , amino acid , materials science , composite material , gene
Phosphorylation at histidine residues occurs frequently in biology, but is often overlooked in proteomics experiments due to extreme acid lability. A new method utilizing histidine labeling with iodine to record information about phosphorylation is described. Essentially, phosphorylated histidine residues are not labeled while unmodified histidine undergoes complete iodination. Iodination is stabile both under acidic conditions, and upon collisional activation in the gas phase. This enables site‐specific information to be retained with standard liquid chromatography separations and tandem mass spectrometry by collisional activation. Semi‐quantitative information about the relative amounts of phosphorylated versus unmodified states can also be easily obtained from the relative ion abundances. This new method should provide a pathway forward for analyzing histidine phosphorylation in complex systems. Copyright © 2011 John Wiley & Sons, Ltd.