4wg2: Difference between revisions
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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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