TABLE 3.
Residues interacting with helix HL and β-sheets
| 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 |
| NK158A | 408 ± 45 (50%) | 489 ± 54 (57%) | 1224 ± 16 (79%) | 0.18 | 0.0028 |
| NK158R | 330 ± 43 (41%) | 350 ± 60 (41%) | 1155 ± 127 (75%) | 0.13 | 0.0022 |
| NH224A | 567 ± 65 (70%) | 623 ± 49 (73%) | 1391 ± 92 (90%) | 0.15 | 0.0032 |
| NV469A | 504 ± 52 (62%) | 612 ± 52 (72%) | 1358 ± 95 (88%) | 0.15 | 0.0031 |
| NVal469stop | 299 ± 13 (37%) | 354 ± 12 (41%) | 970 ± 87 (63%) | 0.18 | 0.0031 |
| NIle475stop | 307 ± 9 (38%) | 237 ± 39 (28%) | 923 ± 88 (60%) | 0.14 | 0.0032 |
| NAla481stop | 505 ± 31 (62%) | 575 ± 28 (67%) | 1267 ± 37 (82%) | 0.15 | 0.0025 |
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).