EC Number   |
Reference |
|---|
    1.7.2.5 | all-atom molecular dynamics simulations within an explicit membrane/solvent environment reveal two possible proton transfer pathways leading from the periplasm to the active site, while no pathways from the cytoplasmic side are found, consistently with the experimental observations that the enzyme is not a proton pump. One of the pathways is blocked in the crystal structure and requires small structural rearrangements to allow for water channel formation. That pathway is equivalent to the functional periplasmic cavity postulated in cbb3 oxidase |
726258 |
| 1.7.2.5 | at cryogenic temperature -173°C wild-type, S286V- and S286T-mutant |
395122 |
| 1.7.2.5 | crystal structure analysis, PDB ID 3O0R |
742714 |
| 1.7.2.5 | in complex with variable heavy chain domain of camel heavy chain antibody, sitting drop vapor diffusion method, using 100 mM potassium phosphate pH 7.0, 0.01% (v/v) phenyl ethanol, 0.005% (v/v) n-dodecyl-beta-D-maltopyranoside |
701110 |
| 1.7.2.5 | in the ferric resting and in the ferrous carbonmonoxy states, at 1.0 and 1.05 A resolution, respectively |
395117 |
| 1.7.2.5 | oxidized S-NOR at 3 A resolution, reduced S-NOR at 2.8 A resolution, NO-reacted S-NOR at 2.8 A resolution |
658125 |
| 1.7.2.5 | sitting drop vapour diffusion, crystals diffract to less than 2.0 A |
659644 |
