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. 2012 Oct 9;109(44):E3035–E3044. doi: 10.1073/pnas.1209039109

Table 2.

Kinetic parameters of Trp fluorescence and 22Na+ binding on WT BetP and mutants

Trp Fluorescence
22Na binding
Site Apparent Kd (mM) Bmax (ΔF/F) n (Hill coefficient) Apparent Kd (mM) n (Hill coefficient)
WT 118 ± 3.9 0.89 ± 0.02 1.9 ± 0.1 53.3 ± 2.1 2.0 ± 0.2
S468A Na2 871 ± 113 0.16 ± 0.05 1.1 ± 0.3 147.5 ± 19 1.0 ± 0.1
T467A/S468A Na2 BD BD BD BD BD
T246L Na1′ 305 ± 28 0.36 ± 0.02 1.9 ± 0.2 167.7 ± 15.5 1.9 ± 0.2
T246L/T250A Na1′ 986 ± 335 0.07 ± 0.03 2.4 ± 0.8 554.8 ± 35.8 1.4 ± 0.1
S376A 191 ± 17 0.72 ± 0.05 1.9 ± 0.2 97.7 ± 5.8 1.8 ± 0.2
W101A/T351A 153.4 ± 23 0.12 ± 0.01 2.0 ± 0.4 59.2 ± 1.5 1.9 ± 0.1

BD, below detection.

Saturation not reached, precluding reliable fitting of the data.

Mutations in the trimer interface.