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. 2012 Dec 7;91(6):1095–1102. doi: 10.1016/j.ajhg.2012.10.008

Table 1.

Redox Properties and Activities of the Wild-Type and Mutants of Mature Human AIF

	WT	p.Glu493Val	p.Arg201del
k_et^NADH (s⁻¹)^a	0.98 ± 0.02	3.9 ± 0.1	23 ± 0.4
K_M^NADH (mM)	1.53 ± 0.06	1.23 ± 0.05	0.23 ± 0.02
t_1/2^CTC (hr)^b	11	1.4	3.4
k_ox^NADH (min⁻¹)^c	0.015 ± 0.002	0.12 ± 0.02	0.06 ± 0.01

DCIP

k_cat (min⁻¹)	137 ± 18	335 ± 32	394 ± 28
K_M^DCIP (μM)	202 ± 36	97 ± 20	16 ± 3
K_M^NADH (mM)	0.74 ± 0.12	0.16 ± 0.04	0.14 ± 0.02
k_cat/ K_M^NADH (mM⁻¹ min⁻¹)	185	2,094	2,814

K₃Fe(CN)₆

k_cat (min⁻¹)	314 ± 25	745 ± 30	1,464 ± 92
K_M^K₃^Fe(CN)₆ (μM)	28 ± 5	26 ± 5	68 ± 6
K_M^NADH (mM)	0.61 ± 0.10	0.26 ± 0.05	0.20 ± 0.03
k_cat/K_M^NADH (mM⁻¹ min⁻¹)	515	2,865	7,320

Cytochrome c

k_cat (min⁻¹)	54 ± 15	35 ± 5	39 ± 2
K_M^{cyt c} (μM)	26 ± 13	28 ± 8	94 ± 10
K_M^NADH (mM)	0.27 ± 0.02	0.15 ± 0.02	0.07 ± 0.01
k_cat/ K_M^NADH (mM⁻¹ min⁻¹)	200	233	557

All activities were determined in 50 mM phosphate buffer (pH 7.4) at 25°C.

^a

The rate constant for the AIF reduction by NADH was determined by stopped flow spectrophotometry at 25°C.

^b

The half-life of the FADH₂-NAD charge-transfer complex (CTC) was determined at 25°C in the presence of 15 μM AIF and 60 μM NADH.

^c

The rate of NADH oxidation by AIF was determined at 25°C.