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Native Electron Capture Dissociation for the Structural Characterization of Noncovalent Interactions in Native Cytochrome c
Author(s) -
Breuker Kathrin,
McLafferty Fred W.
Publication year - 2003
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200351705
Subject(s) - cytochrome c , chemistry , dimer , electron transfer dissociation , electrospray ionization , electron transfer , dissociation (chemistry) , mass spectrometry , ion , non covalent interactions , hemeprotein , heme , electron capture dissociation , photochemistry , stereochemistry , crystallography , tandem mass spectrometry , molecule , mitochondrion , organic chemistry , biochemistry , hydrogen bond , chromatography , enzyme
Selectively cleaved : Under appropriate experimental conditions, electrospray ionization mass spectrometry produces fragment ions that directly indicate noncovalent protein–heme interaction sites in native Cytochrome c (see picture). The proposed mechanism involves asymmetric charge partitioning in gaseous protein dimer ions, which causes electron transfer and subsequent backbone‐cleavage.