EC Number   |
Reference  |
|---|
    1.14.15.1 | Pseudomonas putida PpG786, cytochrome m |
347692 |
| 1.14.15.1 | - |
347696, 347707, 347712 |
| 1.14.15.1 | Pseudomonas sp., ternary complex |
347696 |
| 1.14.15.1 | space group P212121, structure at 2 A resolution |
347703 |
| 1.14.15.1 | structure of the ferrous dioxygen adduct at 0.91 A resolution |
347704 |
| 1.14.15.1 | mutant F87W/Y96F/V247L in complex with 1,3,5-trichlorobenzene or (+)-alpha-pinene |
657898 |
| 1.14.15.1 | mutant Y96F/F87W/V247L, binding of substrate (+)-alpha-pinene in two orientations related by rotation of the molecule |
658971 |
| 1.14.15.1 | purified recombinant wild-type and D251N and T252A mutant enzymes in complex with O2, usage of a high pressure oxygen cell, a single crystal first is transferred into cryobuffer containing 50 mM Tris-HCl, pH 7.4, 0.4-0.6 M KCl, 1 mM D-camphor, 30% polyethylene glycol 4000, and 20% glycerol followed by reduction with 10 mM sodium dithionite for 10 min under anaerobic condition, soaking in the oxygen-saturated cryobuffer at -5°C for 5 min, X-ray diffraction structure determination and analysis at 1.55-2.10 A resolution |
674474 |
| 1.14.15.1 | recombinant wild-type enzyme and mutant L244A/C334A in complex with imidazole or 1-methylimidazole, hanging drop vapour diffusion method, purified recombinant protein in 50 mM potassium phosphate, 250 mM KCl, 50 mM DTT, and 36-52% ammonium sulfate, mixing with an equal volume of 0.001 ml of mother liquor containing 25 mM imidazole or 1-methylimidazole, room temperature, 2 days, cryoprotectant is 50 mM KCl, 25% ammonium sulfate and 30% glycerol, X-ray diffraction structure determination and analysis at 1.5-2.15 A resolution |
676941 |
| 1.14.15.1 | two ferric P450cam structures partially complexed with (+)-camphor, by sitting-drop vapour-diffusion method, at 1.3 A (soaked crystals) or 1.35 A (unsoaked crystals) resolution. Belongs to space group P43212, unsoaked crystals have unit-cell parameters of a = b = 63.38, c = 247.30, whereas soaked crystals have unit-cell parameters of a = b = 63.61 and c = 250.39. Structure of the unsoaked P450cam shows an active site that is partially occupied by (+)-camphor and a water molecule liganded to the haem iron and rotamers of Thr101. (+)-Camphor-bound form is the major component and the water-bound form is the minor component. In the soaked P450cam, the population of the major component increases, while the minor component decreases. (+)-Camphor binding induces rotation of Thr101 to form a hydrogen bond that acts as a hydrogen donor to a peripheral haem propionate. This bonding contributes to redox-potential change |
701533 |
