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. Author manuscript; available in PMC: 2014 Oct 29.
Published in final edited form as: Biochemistry. 2013 Oct 14;52(43):10.1021/bi401132w. doi: 10.1021/bi401132w

Table 4.

DNA binding affinities of the indicated metallated derivatives of wild-type and mutant PsaRs as analyzed by a dimer linkage modela

Spn PsaR log KDNA (M−1) Fractional change in KDNA from
corresponding wild-type PsaR		 ΔGc (kcal mol−1)
wild-type PsaRZn,apo 6.2 (±0.1) 1 —
wild-type PsaRZn,Zn 8.02 (±0.03) 0.0027b −2.5 (±0.2)d
wild-type PsaRZn,Mn 10.6 (±0.1) 1 −6.0 (±0.3)d
wild-type PsaRMn,Mn 10.1 (±0.1) 0.30 −5.4 (±0.4)d
D7A PsaRZn,apo 6.73 (±0.05) 3.6c —
D7A PsaRZn,Mn 7.22 (±0.03) 0.00042 −0.7 (±0.1)e
E99A PsaRZn,apo 6.7 (±0.1) 3.6 —
E99A PsaRZn,Mn 9.27 (±0.05) 0.048 −3.5 (±0.2)e
H125A PsaRZn,apo 7.39 (±0.04) 16 —
H125A PsaRZn,Mn 10.4 (±0.1) 0.71 −4.1 (±0.2)e
D160A PsaRZn,apo 6.58 (±0.06) 2.5 —
D160A PsaRZn,Mn 9.8 (±0.1) 0.17 −4.4 (±0.2)e
H76A PsaRZn,apo 6.3 (±0.2) 1.4 —
H76A PsaRZn,Mn 9.6 (±0.1) 0.11 −4.5 (±0.4)e
H76F PsaRZn,apo 6.2 (±0.1) 1.0 —
H76F PsaRZn,Mn 8.54 (±0.06) 0.0089 −3.2 (±0.2)e
a

Determined from experiments like those shown in Fig. 5 with the numbers in parentheses defined as the unweighted standard error of the fit from triplicate titrations.

b

The numbers in standard text are calculated from KDNA(mutant PsaRi,j)/KDNA(wild-type PsaRZn,apo), where i=j=Zn or Mn.

c

The numbers in italicized font are given by the ratio KDNA(mutant PsaRZn,apo)/KDNA(wild-type PsaRZn,apo).

d

ΔGc= −RTln(KDNA(wild-type PsaRi,j)/KDNA(wild-type PsaRZn,apo), where i=j=Zn or Mn.

e

ΔGc= −RTln(KDNA(mutant PsaRZn,Mn)/KDNA(mutant PsaRZn,apo).