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It is also noticeable that the unimolecular fragmentation
of protonated homo- and heterodimeric disulfides shows
both some similarity to and some important differences from
that of protonated bis-thiolatomercury(II) compounds.18 The
most striking difference is lack of abundant [MH ꢀ NH3]C
first-generation fragments in the spectra of the homo-
and heterodimeric disulfides of cysteine and penicillamine,
which are on the contrary observed in the corresponding
mercury-bridged compounds at the same value of collision
energy. Although the reasons for this difference are not
fully understood, it is nevertheless conceivable that binding
to mercury (a more electropositive element than sulfur)
enhances the nucleophilicity of the sulfur atom with respect
to that of the disulfide bond, thus favouring the displacement
of ammonia. On the other hand, the important similarities
observed in the unimolecular reactivity of protonated
disulfides and mercury conjugates of sulfur amino acids
and peptides, such as the formation of amino acid sulfenium
fragments, strengthens the in vitro evidence that intracellular
mercury uptake mediated by a specific anion transporter in
the kidney cells may occur by stereoelectronic mimickry of
cystine by cysteine–mercury(II) thiolate conjugates.30
14. Fagerquist CK. Collision-activated cleavage of
a
pep-
tide/antibiotic disulfide linkage: possible evidence for
intramolecular disulfide bond rearrangement upon collisional
activation. Rapid Commun. Mass Spectrom. 2004; 18: 685.
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18. Rubino FM, Verduci C, Giampiccolo R, Pulvirenti S, Bram-
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Finally, the reported spectroscopic information can be
used specifically to detect and measure amino acid and
glutathione disulfides present in biological samples analyzed
by liquid chromatography and tandem mass spectrometry.
19. Reid GE, Simpson RJ, O’Hair RAJ. Leaving group and gas
phase neighboring group effects in the side chain losses from
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Copyright 2004 John Wiley & Sons, Ltd.
J. Mass Spectrom. 2004; 39: 1408–1416