EC Number   |
|---|
    1.14.14.18 | - |
| 1.14.14.18 | apo- and heme-bound truncated HO-2, lacking the three heme regulatory motifs and the membrane binding region, apo-HO-2: hanging drop method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 40% PEG 1500, 200 mM potassium glutamate, and 100 mM triethanolamine, pH 8.5, at 4°C, heme-bound HO-2: hanging drop vapour diffusion method, 0.0015 ml of 5 mg/ml protein in 50 mM KCl, 50 mM Tris-HCl, pH 7.5, are mixed with 0.001 ml of well solution containing 33% PEG dimethlyether 500, 20 mM MgCl2, and 100 mM HEPES, pH 8.5, at 4°C, X-ray diffraction structure determination and analysis at 2.4 A resolution for the apoenzyme, and at 2.6 A resolution for the heme-bound enzyme |
| 1.14.14.18 | apo-enzyme and in complex with heme |
| 1.14.14.18 | azide-bound Fe(II)-verdoheme-HmuO, 30°C, a hanging drop vapor diffusion method, the reservoir solution containing 50 mM MES, pH 5.4, 2.3-2.5 M ammonium sulfate, 0.27 M sodium bromide, and 0.1% dioxane, X-ray diffraction structure determination and analysis at 3.0 A resolution |
| 1.14.14.18 | crystal structure at 1.5 A resolution, comparison with heme oxygenase-1 from mammalian sources |
| 1.14.14.18 | crystal structure determination and analysis of HO-1 in complex with different inhibitors, i.e. 2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl) methyl]-1,3-dioxolane, (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4-[((5-trifluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane, 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone, 4-phenyl-1-(1,2,4-1H-triazol-1-yl)butan-2-one, and 1-(1H-imidazol-1-yl)-4,4-diphenyl-2-butanone, overview |
| 1.14.14.18 | dioxygen bound form |
| 1.14.14.18 | DTT-bound forms of ferric heme-HO-1 complexes, X-ray diffraction structure analysis of crystal structures with PDB IDSs I9T and 3I9U, resolution is 1.5 A |
| 1.14.14.18 | ferric and ferrous forms of the heme complex |
| 1.14.14.18 | hanging drop vapor diffusion method, free enzyme is crystallized by using 85 mM sodium cacodylate, pH 6.5, 25.5% (w/v) PEG8000, 170 mM sodium acetate, and 23.5% (v/v) glycerol, while substrate-bound enzyme is crystallized by using 50 mM MES, pH 6.1, 2.2 M ammonium sulfate, and 25% (w/v) sucrose, supplemented with 200 mM sodium ascorbate |
