EC Number   |
Title |
Organism |
|---|
   1.11.2.4 | Aromatic C-H bond hydroxylation by P450 peroxygenases: a facile colorimetric assay for monooxygenation activities of enzymes based on Russigs blue formation |
Bacillus subtilis |
| 1.11.2.4 | Crystallization and preliminary X-ray diffraction analysis of fatty-acid hydroxylase cytochrome P450BSbeta from Bacillus subtilis |
Bacillus subtilis |
| 1.11.2.4 | Cytochrome P450 monooxygenase from Clostridium acetobutylicum: a new alpha-fatty acid hydroxylase |
Clostridium acetobutylicum |
| 1.11.2.4 | Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy |
Sphingomonas paucimobilis |
| 1.11.2.4 | Enzymatic reaction of hydrogen peroxide-dependent peroxygenase cytochrome P450s: kinetic deuterium isotope effects and analyses by resonance Raman spectroscopy |
Bacillus subtilis |
| 1.11.2.4 | Functional modulation of a peroxygenase cytochrome P450: novel insight into the mechanisms of peroxygenase and peroxidase enzymes |
Bacillus subtilis |
| 1.11.2.4 | Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3 |
Fusarium oxysporum |
| 1.11.2.4 | Fusarium oxysporum fatty-acid subterminal hydroxylase (CYP505) is a membrane-bound eukaryotic counterpart of Bacillus megaterium cytochrome P450BM3 |
Fusarium oxysporum MT-811 |
| 1.11.2.4 | Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes |
Sphingomonas paucimobilis |
| 1.11.2.4 | Peroxide-utilizing biocatalysts: structural and functional diversity of heme-containing enzymes |
Bacillus subtilis |
