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. Author manuscript; available in PMC: 2016 Aug 5.
Published in final edited form as: Biochemistry. 2016 Apr 20;55(17):2452–2464. doi: 10.1021/acs.biochem.5b01373

Figure 3. Nitrosation of human and yeast GSNORs also depends on conserved cysteine residues.

Figure 3

A. Multiple sequence alignment of GSNORs examined in this study. Black boxes denote zinc-coordinating cysteines, while yellow stars indicate putative nitrosation sites according to GPS SNO [34]. B-I: Deconvolved mass spectra of wild-type and cysteine mutant human GSNOR (B-E) and the yeast ortholog SFA1 (F-I) treated with the NO donor CysNO. Black (▶) and red (Inline graphic) arrowheads designate unmodified GSNOR and nitrosated GSNOR adducts (+29 Da), respectively. J-K: Yeast alcohol dehydrogenase 1 (ADH1) is not nitrosated under the same conditions. The green circle (Inline graphic) demarcates an unknown 16 Da adduct in the CysNO-treated sample.