4H24
Cytochrome P450BM3-CIS cyclopropanation catalyst
Summary for 4H24
| Entry DOI | 10.2210/pdb4h24/pdb |
| Related | 4H23 |
| Descriptor | Cytochrome P450-BM3 variant P450BM3-Cis, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| Functional Keywords | cytochrome p450, enzymatic cyclopropanation, directed evolution, non-natural function, oxidoreductase |
| Biological source | Bacillus megaterium |
| Cellular location | Cytoplasm (By similarity): P14779 |
| Total number of polymer chains | 4 |
| Total formula weight | 217419.23 |
| Authors | Coelho, P.S.,Wang, Z.J.,Ener, M.E.,Baril, S.A.,Kannan, A.,Arnold, F.H.,Brustad, E.M. (deposition date: 2012-09-11, release date: 2013-06-26, Last modification date: 2023-09-20) |
| Primary citation | Coelho, P.S.,Wang, Z.J.,Ener, M.E.,Baril, S.A.,Kannan, A.,Arnold, F.H.,Brustad, E.M. A serine-substituted P450 catalyzes highly efficient carbene transfer to olefins in vivo. Nat.Chem.Biol., 9:485-487, 2013 Cited by PubMed Abstract: Whole-cell catalysts for non-natural chemical reactions will open new routes to sustainable production of chemicals. We designed a cytochrome 'P411' with unique serine-heme ligation that catalyzes efficient and selective olefin cyclopropanation in intact Escherichia coli cells. The mutation C400S in cytochrome P450(BM3) gives a signature ferrous CO Soret peak at 411 nm, abolishes monooxygenation activity, raises the resting-state Fe(III)-to-Fe(II) reduction potential and substantially improves NAD(P)H-driven activity. PubMed: 23792734DOI: 10.1038/nchembio.1278 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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