. Author manuscript; available in PMC: 2016 Sep 12.

Published in final edited form as: Biochemistry. 2014 Dec 22;54(2):490–496. doi: 10.1021/bi501266e

Table 2.

Kinetic Constants of the Quinone Reductase Activity for NqrB-D397N and Wild-Type Na⁺-NQR Obtained in the Presence of Na⁺, Li⁺, and K⁺^a

		k_cat (s⁻¹)	K_m (mM)	k_cat/K_m (mM/s)
NaCl	wild type	500 ± 42	2.5 ± 0.9	200 ± 73.9
	NqrB-D397N	127 ± 15	3.1 ± 1.1	41 ± 15.3
LiCl	wild type	180 ± 25	3.5 ± 1.1	51.4 ± 17.67
	NqrB-D397N	100 ± 15	2.4 ± 1.2	41.6 ± 21.75
KC1	wild type	ND^b	ND^b	ND^b
	NqrB-D397N	109 ± 8.4	53.7 ± 16.8	2.03 ± 0.65

The kinetic constants were determined from the saturation curves using the Michaelis–Menten equation. Each titration curve is the result of at least seven independent repetitions. The standard deviations are presented. In each repetition, every point was measured in triplicate. Conditions of the measurements are described in Materials and Methods.

Not detected.