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. 2020 Sep 22;21(18):6949. doi: 10.3390/ijms21186949

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© 2020 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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pK_a and hydrophobic effects on the observed hyper-reactivity toward GSSG in different proteins. (A) Experimental kinetic data for the reaction of Cys75 for rBSA, Cys94 for rLyz, Cys95 for rRNase and Cys1 for rChTg with GSSG normalized to those of an unperturbed protein cysteine (enhanced reactivity) [13,14,15,16]. (B) Enhanced reactivity due to the experimental lower pK_a of the protein cysteines of panel (A) (pK_a values: 6.6 for Cys75, 6.6 for Cys94, 7.9 for Cys95 and 8.1 for Cys1) [13,14,15,16]. (C) Enhanced reactivity due to a transient complex. (D) Circle diagrams show the percent contribution of the two factors: transient complex protein-GSSG (blue) and pK_a effect (red). The 100% represents the sum of the values reported in panel (B,C). The error bars in panels (A–C) derived from the propagation of uncertainties (see Section 4).