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. Author manuscript; available in PMC: 2012 Jun 8.
Published in final edited form as: Nature. 2010 Dec 23;468(7327):1115–1118. doi: 10.1038/nature09599

Figure 2. Cysteine mutants (C689S, C908S and C689S/C908S) of heNOS resist S-glutathionylation and secondary uncoupling.

Figure 2

WT heNOS and heNOS C689S, C908S and C689S/C908S mutants were treated with 2 mM GSSG. a, Percentage loss of NOS activity after treatment of heNOS with GSSG. b, Percentage increase in O2•− generation after treatment of heNOS with GSSG. c, Ratio of relative eNOS S-glutathionylation to eNOS protein. The relative intensity of eNOS S-glutathionylation/eNOS protein was normalized to the wild-type value. The Cys→Ser mutants maintained a NOS activity similar to that of the wild type (120 ± 12 n mol min−1 mg−1). Results are shown as means and s.e.m. (n =3).