Skip to main content
. Author manuscript; available in PMC: 2015 Feb 1.
Published in final edited form as: Biochim Biophys Acta. 2013 Jun 6;1840(2):847–875. doi: 10.1016/j.bbagen.2013.05.040

Table 6.

Rate constants for sulfenic acid-mediated disulfide formation and thiol-mediated reactivation of enzymes.

Reaction Rate Constant Conditions References
R-SOH + R′-SH → R-S-S-R′
Cys-SOH + Cys >105 M−1 s−1 18 °C, pH 7.0 [79]
Cdc25B-SOH + back-door Cys 0.16 s−1 20 °C, pH 7.0 [180]
Cdc25C-SOH + back-door Cys 0.012 s−1 20 °C, pH 7.0 [180]
HSA-SOH + Cys 21.6 M−1 s−1 25 °C, pH 7.4 [177]
HSA-SOH + GSH 2.9 M−1 s−1 25 °C, pH 7.4 [177]
Reactivation of enzyme
MKP3ox + GSH/Trx-TrxR 1–2/316 M−1 s−1 20 °C, pH 8.0 [199]
Cdc25Box + DTT/Trx-TrxR 0.5/1007 M−1 s−1 20 °C, pH 7.0 [180]
PTP-SSG + Grx 483 M−1 s−1 30 °C, pH 7.0 [201]
SHP-1 + DTT/GSH 0.64/0.026 25 °C, pH 7.5 [198]
SHP-2 + DTT/GSH 0.46/0.16 25 °C, pH 7.5 [198]
ΔSHP-1 + DTT/GSH 0.33/0.077 25 °C, pH 7.5 [198]
ΔSHP-2 + DTT/GSH 0.84/0.07 25 °C, pH 7.5 [198]