. Author manuscript; available in PMC: 2014 Apr 1.

Published in final edited form as: Metallomics. 2013 Apr;5(4):335–342. doi: 10.1039/c3mt20205d

Table 2.

Summary of binding constants obtained from fluorescence anisotropy experiments of WT CstR or CstR cysteine mutants with cst OP1

Protein	r₀	r_complex	K_tet (M⁻¹) × 10⁻⁷
CstR	0.133	0.155	6.3 (± 0.5)
CstR + SeO₃²⁻	0.132	0.154^*	0.20 (± 0.03)
CstR + TeO₃²⁻	0.133	0.155^*	0.13 (± 0.14)
CstR + S₄O₆²⁻	0.132	0.154^*	0.11 (± 0.11)
C31A CstR	0.135	0.161	3.3 (± 0.7)
C31A CstR + MMTS	0.135	0.159	2.0 (± 0.5)
C60A CstR	0.135	0.159	4.2 (± 1.0)
C60A CstR + MMTS	0.136	0.158^*	0.31 (± 0.03)
C31A/C60A CstR	0.134	0.157	12 (± 5)

Fit to Δ anisotropy of corresponding non-derivatized CstR