4WG2
P411BM3-CIS T438S I263F regioselective C-H amination catalyst
Summary for 4WG2
| Entry DOI | 10.2210/pdb4wg2/pdb |
| Related | 4H23 |
| Descriptor | Bifunctional P-450/NADPH-P450 reductase, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| Functional Keywords | p411bm3-cis, engineering, catalysis, oxidoreductase |
| Biological source | Bacillus megaterium |
| Cellular location | Cytoplasm : P14779 |
| Total number of polymer chains | 3 |
| Total formula weight | 162970.83 |
| Authors | Hyster, T.K.,Farwell, C.C.,Buller, A.R.,McIntosh, J.A.,Arnold, F.H. (deposition date: 2014-09-17, release date: 2014-11-05, Last modification date: 2023-12-27) |
| Primary citation | Hyster, T.K.,Farwell, C.C.,Buller, A.R.,McIntosh, J.A.,Arnold, F.H. Enzyme-controlled nitrogen-atom transfer enables regiodivergent C-h amination. J.Am.Chem.Soc., 136:15505-15508, 2014 Cited by PubMed Abstract: We recently demonstrated that variants of cytochrome P450BM3 (CYP102A1) catalyze the insertion of nitrogen species into benzylic C-H bonds to form new C-N bonds. An outstanding challenge in the field of C-H amination is catalyst-controlled regioselectivity. Here, we report two engineered variants of P450BM3 that provide divergent regioselectivity for C-H amination-one favoring amination of benzylic C-H bonds and the other favoring homo-benzylic C-H bonds. The two variants provide nearly identical kinetic isotope effect values (2.8-3.0), suggesting that C-H abstraction is rate-limiting. The 2.66-Å crystal structure of the most active enzyme suggests that the engineered active site can preorganize the substrate for reactivity. We hypothesize that the enzyme controls regioselectivity through localization of a single C-H bond close to the iron nitrenoid. PubMed: 25325618DOI: 10.1021/ja509308v PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.66 Å) |
Structure validation
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