EC Number |
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7.1.1.6 | - |
7.1.1.6 | 3.0 A crystal structure, native enzyme and enzyme in complex with 8-hydroxy-5,7-dimethoxy-3-methyl-2-tridecyl-4H-chromen-4-one or with 2,5-dibromo-5-methyl-6-isopropyl-benzoquinone |
7.1.1.6 | free enzyme and enzyme complexed with with quinone analogue inhibitors tridecyl-stigmatellin and 2-nonyl-4-hydroxyquinoline N-oxide, X-ray diffraction structure determination at 2.70 A, 3.07 A, and 3.25 A resolution, respectively |
7.1.1.6 | hanging drop vapour diffuion method, 0.0015 ml protein solution, containing 0.135-0.18 mM protein, is mixed with 0.0015 ml of reservoir solution, containing 100 mM Tris-HCl, pH 8.5, 200 mM MgCl2, 40 mM CdCl2, and 16?17% PEG-550 monomethyl ether, 4 °C, hexagonal bipyramidal crystals appear in 24?36 h, X-ray diffraction structure determination at 2.8 A resolution |
7.1.1.6 | hanging drop vapour diffusion method using 1.5 M [NH4]2SO4, 100 mM sodium acetate at pH 4.6 |
7.1.1.6 | hanging drop, vapor-diffusion method |
7.1.1.6 | hanging-drop vapor diffusion. A native structure of the cytochrome b6f complex with improved resolution is obtained from crystals of the complex grown in the presence of divalent cadmium |
7.1.1.6 | modeling of the first step of plastoquinol PQH2 oxidation by the iron-sulfur protein of the Cyt b6f complex. The H-transfer reaction displays a bidirectional mechanism, an electron is directed to the Fe(1) atom of the [Fe2S2] cluster of the iron-sulfur protein, and a proton is accepted by the Nepsilon atom of the His155 residue liganding the Fe(1) atom. Results support a diabatic model of the H-transfer, which implies that the elementary steps of electron and proton transfer occur much more rapidly than the concomitant changes in the system geometry |
7.1.1.6 | vapour diffusion hanging drop method, X-ray structure at 3.1 A |