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4wg2
From Proteopedia
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| - | ''' | + | ==P411BM3-CIS T438S I263F regioselective C-H amination catalyst== |
| + | <StructureSection load='4wg2' size='340' side='right' caption='[[4wg2]], [[Resolution|resolution]] 2.66Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4wg2]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WG2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WG2 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4h23|4h23]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4wg2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wg2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wg2 RCSB], [http://www.ebi.ac.uk/pdbsum/4wg2 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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-A 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. | ||
| - | + | Enzyme-Controlled Nitrogen-Atom Transfer Enables Regiodivergent C-H Amination.,Hyster TK, Farwell CC, Buller AR, McIntosh JA, Arnold FH J Am Chem Soc. 2014 Oct 24. PMID:25325618<ref>PMID:25325618</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Arnold, F H.]] | ||
| + | [[Category: Buller, A R.]] | ||
| + | [[Category: Farwell, C C.]] | ||
| + | [[Category: Hyster, T K.]] | ||
| + | [[Category: McIntosh, J A.]] | ||
| + | [[Category: Catalysis]] | ||
| + | [[Category: Engineering]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: P411bm3-cis]] | ||
Revision as of 08:49, 5 November 2014
P411BM3-CIS T438S I263F regioselective C-H amination catalyst
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