8D1C
Crystal structure of T252E-CYP199A4 in complex with 4-(Trifluoromethoxy)benzoic acid
Summary for 8D1C
| Entry DOI | 10.2210/pdb8d1c/pdb |
| Descriptor | Cytochrome P450, PROTOPORPHYRIN IX CONTAINING FE, 4-(trifluoromethoxy)benzoic acid, ... (5 entities in total) |
| Functional Keywords | cytochrome, bacterial p450, 4-trifluoromethoxybenzoic acid, oxidoreductase |
| Biological source | Rhodopseudomonas palustris |
| Total number of polymer chains | 1 |
| Total formula weight | 45473.50 |
| Authors | Lee, J.H.Z.,Bruning, J.B.,Bell, S.G. (deposition date: 2022-05-27, release date: 2023-03-01, Last modification date: 2023-10-25) |
| Primary citation | Lee, J.H.Z.,Podgorski, M.N.,Moir, M.,Gee, A.R.,Bell, S.G. Selective Oxidations Using a Cytochrome P450 Enzyme Variant Driven with Surrogate Oxygen Donors and Light. Chemistry, 28:e202201366-e202201366, 2022 Cited by PubMed Abstract: Cytochrome P450 monooxygenase enzymes are versatile catalysts, which have been adapted for multiple applications in chemical synthesis. Mutation of a highly conserved active site threonine to a glutamate can convert these enzymes into peroxygenases that utilise hydrogen peroxide (H O ). Here, we use the T252E-CYP199A4 variant to study peroxide-driven oxidation activity by using H O and urea-hydrogen peroxide (UHP). We demonstrate that the T252E variant has a higher stability to H O in the presence of substrate that can undergo carbon-hydrogen abstraction. This peroxygenase variant could efficiently catalyse O-demethylation and an enantioselective epoxidation reaction (94 % ee). Neither the monooxygenase nor peroxygenase pathways of the P450 demonstrated a significant kinetic isotope effect (KIE) for the oxidation of deuterated substrates. These new peroxygenase variants offer the possibility of simpler cytochrome P450 systems for selective oxidations. To demonstrate this, a light driven H O generating system was used to support efficient product formation with this peroxygenase enzyme. PubMed: 35712785DOI: 10.1002/chem.202201366 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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