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. 2015 Jul 1;290(34):20761–20773. doi: 10.1074/jbc.M115.660381

TABLE 1.

Activity measurements of 11 double cysteine mutants that include the L subunit lateral helix

Mutation Distancea Deamino-NADH oxidase activityb % Deamino-NADH oxidase activityc Ferricyanide reductase activityb % Ferricyanide reductase activityc
Å nmol/mg protein/min nmol/mg protein/min
pBA400 165 ± 48 (15)c 100 710 ± 200 (8)c 100
A557C(L) + A307C(M) 4.92 137 ± 29 (5) 83 744 ± 45 105
K561C(L) + A307C(M) 4.22 133 ± 11 (5) 81 770 ± 55 108
L565C(L) + P239C(M) 5.43 160 ± 59 (5) 97 765 ± 15 108
K561C(L) + D163C(M) 12.05 270 ± 10 (2) 164 797 ± 12 112
N570C(L) + D163C(M) 13.63 161 ± 3 (2) 98 643 ± 22 91
N570C(L) + D246C(M) 10.86 250 ± 12 (2) 151 853 ± 15 120
V574C(L) + D246C(M) 16.12 230 ± 14 (2) 139 905 ± 13 128
K581C(L) + S290C(N) 6.22 138 ± 5 (2) 84 690 ± 43 97
L594C(L) + L225C(N) 4.46 86 ± 11 (2) 52 651 ± 21 92
S597C(L) + L225C(N) 5.7 161 ± 5 (2) 98 940 ± 43 132
D546C(L) + D241C(L) 13.04 230 ± 5 (2) 139 745 ± 62 105
BA14 18 ± 3 (2) 11 84 ± 2 12

a Distance between the α-carbons of the native residues.

b Activity was measured in membrane preparations as described under “Experimental Procedures.” The means, S.D., and number of measurements (parentheses) are shown. For ferricyanide reductase activity, two-three measurements were made except for wild type and BA14.

c Activity is expressed as a percentage of the wild type rate.