. 2019 Jul 2;476(13):1875–1887. doi: 10.1042/BCJ20190095

Table 1. Dissociation constant (K_d) values for the ChlD–ChlH interaction of the ChlD mutants.

ChlD mutant	Mutation type	Mg²⁺ present K_d/µM	Mg²⁺ free K_d/µM
Wild type		0.331 ± 0.058	2.10 ± 0.387
Truncation A	N-terminal truncation ⁽¹⁾ AAA⁺ domain alone	14.6 ± 2.99	5.93 ± 1.08
Truncation B	N-terminal truncation⁽¹⁾ AAA⁺ and PP domain	10.5 ± 1.9	6.76 ± 1.52
QuinE	Allosteric response to Mg^{2+ (2)}	0.339 ± 0.040	0.512 ± 0.161
D487E	MIDAS motif	0.842 ± 0.162	1.489 ± 0.221
S489A	MIDAS motif	1.98 ± 0.52	3.21 ± 0.76
S491A	MIDAS motif	0.147 ± 0.026	0.351 ± 0.097
S554R	MIDAS motif	0.481 ± 0.140	0.988 ± 0.126

K_d reported to three significant figures, errors reported as ± the estimated standard deviation of the K_d. Each K_d is determined from three independent biological repeats, errors reported are from non-linear regression. Constructs originally described in (1) Adams et al. [11] and (2) Brindley et al. [13].

Table 1. Dissociation constant (Kd) values for the ChlD–ChlH interaction of the ChlD mutants.

Table 1. Dissociation constant (K_d) values for the ChlD–ChlH interaction of the ChlD mutants.