TABLE 1.
Conserved charged residues in the TM of NuoN, NuoM, and NuoL potentially involved in energy transduction
| Mutation | dNADH-O2a | dNADH-DBa | dNADH-K3Fe(CN)6b | IC50 (cap)c | IC50 (squ)d |
|---|---|---|---|---|---|
| WT | 812 ± 25 (100%) | 854 ± 37 (100%) | 1546 ± 27 (100%) | 0.19 | 0.0023 |
| NKO | 5 ± 2 (0.6%) | 15 ± 2 (2%) | 394 ± 29 (25%) | ||
| NKO-rev | 772 ± 74 (95%) | 850 ± 81 (100%) | 1565 ± 107 (101%) | 0.20 | 0.0061 |
| NE133A | 584 ± 42 (72%) | 753 ± 136 (88%) | 1576 ± 93 (102%) | 0.21 | 0.0040 |
| NE133A/KKO | 6 ± 1 (0.7%) | 18 ± 2 (2%) | 306 ± 56 (20%) | ||
| NE133A/KKO-rev | 615 ± 5 (76%) | 804 ± 61 (94%) | 1497 ± 56 (97%) | 0.20 | 0.0054 |
| NE133A/KE72A | 163 ± 15 (20%) | 164 ± 5 (19%) | 1095 ± 41 (71%) | 0.13 | 0.0029 |
| KKO | (1%)e | (7%)e | (14%)e | ||
| KE72A | (43%)e | (48%)e | (103%)e | 0.12e | |
| NK217A | 428 ± 42 (53%) | 473 ± 61 (55%) | 1425 ± 169 (92%) | 0.19 | 0.0030 |
| NK217C | 498 ± 53 (61%) | 484 ± 24 (57%) | 1584 ± 141 (102%) | 0.18 | 0.0052 |
| NK217R | 395 ± 37 (49%) | 374 ± 27 (44%) | 1344 ± 79 (87%) | 0.19 | 0.0038 |
| NK247A | 256 ± 21 (32%) | 274 ± 24 (32%) | 1088 ± 65 (70%) | 0.19 | 0.0028 |
| NK247R | 615 ± 91 (76%) | 799 ± 110 (94%) | 1565 ± 134 (101%) | 0.23 | 0.0043 |
| NK395A | 15 ± 2 (2%) | 30 ± 3 (4%) | 1092 ± 113 (71%) | ||
| NK395R | 348 ± 41 (43%) | 317 ± 21 (37%) | 1397 ± 93 (90%) | 0.19 | 0.0024 |
| MKO | 6 ± 2.4 (0.7%) | 12 ± 1 (1.4%) | 368 ± 23 (24%) | ||
| ME407A | 42 ± 5 (5%) | 72 ± 10 (8%) | 1007 ± 38 (65%) | ||
| LKO | 26 ± 4 (3%) | 50 ± 8 (6%) | 859 ± 120 (56%) | ||
| LR175A | 131 ± 8 (16%) | 147 ± 7 (17%) | 926 ± 10 (60%) | 0.17 | 0.0034 |
| LK342A | 92 ± 3 (11%) | 94 ± 11 (11%) | 968 ± 6 (63%) | 0.18 | 0.0023 |
a Activity in nanomole of dNADH/mg of protein/min.
b Activity in nanomole of K3Fe(CN)6/mg of protein/min.
c Concentration of capsaicin-40 (cap) that causes 50% inhibition on dNADH-oxidase activity (μm).
d Concentration of squamotacin (squ) that causes 50% inhibition on dNADH-oxidase activity (μm).
e From Ref. 26.