EC Number |
Reference |
---|
1.11.1.19 | batch method, using 0.89 M ammonium sulfate, 0.92 M sodium chloride, at 10°C |
712362 |
1.11.1.19 | deglycosylated DyP is crystallized by the batch method, using 0.92 M NaCl and 0.89 M ammonium sulfate as precipitant |
710721 |
1.11.1.19 | deglycosylated DyP is crystallized by the sitting drop vapor diffusion method, using 25.3% (w/v) PEG 8000 at 5.5 K (pH 6.2) |
710722 |
1.11.1.19 | enzyme in the absence of substrate as well as in the presence of potassium cyanide and veratryl alcohol, hanging drop vapor diffusion method, using 2.4 M sodium malonate pH 7.0 |
764924 |
1.11.1.19 | hanging drop vapor diffusion method, using 32.5% (w/v) PEG 4000 as precipitant |
741854 |
1.11.1.19 | HEPES-bound enzyme, sitting drop vapor diffusion method, using 25% (v/v) 2-methyl-2,4-pentanediol, 50 mM HEPES, pH 7.0 |
764030 |
1.11.1.19 | in complex with heme, hanging drop vapor diffusion method, using 0.2 M ammonium sulfate, 20% (w/v) PEG3350 and 0.1 M Bis-Tris pH 5.5 |
741833 |
1.11.1.19 | in complex with veratryl alcohol |
764888 |
1.11.1.19 | resonance Raman and electrochemical study. In solution, enzyme shows a heterogeneous spin population, with the six-coordinated low-spin state being the most populated. The poor catalytic activity of BsDyP is ascribed to the presence of a catalytically incompetent six-coordinated low-spin population. The spin population is sensitively dependent on the pH, temperature, and physical, i.e., solution versus crystal versus immobilized, state of the enzymes. The redox potential for the Fe2+/Fe3+ couple is -40 mV at pH 7.6, which is substantially more positive than those reported for the majority of other peroxidases |
724379 |
1.11.1.19 | sitting drop vapor diffusion method, using 0.2 M ammonium acetate, 0.1 M sodium acetate trihydrate and 34% (w/v) PEG 4000 |
764354 |