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==Structure of Ene-reductase 1 NostocER1 from cyanobacteria== | |||
<StructureSection load='6uff' size='340' side='right'caption='[[6uff]], [[Resolution|resolution]] 2.01Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6uff]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Nostoc_sp._PCC_7120_=_FACHB-418 Nostoc sp. PCC 7120 = FACHB-418]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UFF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UFF FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.007Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6uff FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uff OCA], [https://pdbe.org/6uff PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uff RCSB], [https://www.ebi.ac.uk/pdbsum/6uff PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uff ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8YVV8_NOSS1 Q8YVV8_NOSS1] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Flavin-dependent 'ene'-reductases (EREDs) are highly selective catalysts for the asymmetric reduction of activated alkenes. This function is, however, limited to enones, enoates, and nitroalkenes using the native hydride transfer mechanism. Here we demonstrate that EREDs can reduce vinyl pyridines when irradiated with visible light in the presence of a photoredox catalyst. Experimental evidence suggests the reaction proceeds via a radical mechanism where the vinyl pyridine is reduced to the corresponding neutral benzylic radical in solution. DFT calculations reveal this radical to be "dynamically stable", suggesting it is sufficiently long lived to diffuse into the enzyme active site for stereoselective hydrogen atom transfer. This reduction mechanism is distinct from the native one, highlighting the opportunity to expand the synthetic capabilities of existing enzyme platforms by exploiting new mechanistic paradigms. | |||
Photoenzymatic Hydrogenation of Heteroaromatic Olefins using 'Ene'-Reductases with Photoredox Catalysts.,Hyster T, Nakano Y, Black MJ, Meichan AJ, Sandoval BA, Chung M, Biegasiewicz K, Zhu T Angew Chem Int Ed Engl. 2020 Mar 17. doi: 10.1002/anie.202003125. PMID:32181943<ref>PMID:32181943</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6uff" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Nostoc sp. PCC 7120 = FACHB-418]] | |||
[[Category: Hyster T]] | |||
[[Category: Jeffrey PD]] | |||
[[Category: Sandoval B]] | |||
Latest revision as of 10:50, 11 October 2023
Structure of Ene-reductase 1 NostocER1 from cyanobacteriaStructure of Ene-reductase 1 NostocER1 from cyanobacteria
Structural highlights
FunctionPublication Abstract from PubMedFlavin-dependent 'ene'-reductases (EREDs) are highly selective catalysts for the asymmetric reduction of activated alkenes. This function is, however, limited to enones, enoates, and nitroalkenes using the native hydride transfer mechanism. Here we demonstrate that EREDs can reduce vinyl pyridines when irradiated with visible light in the presence of a photoredox catalyst. Experimental evidence suggests the reaction proceeds via a radical mechanism where the vinyl pyridine is reduced to the corresponding neutral benzylic radical in solution. DFT calculations reveal this radical to be "dynamically stable", suggesting it is sufficiently long lived to diffuse into the enzyme active site for stereoselective hydrogen atom transfer. This reduction mechanism is distinct from the native one, highlighting the opportunity to expand the synthetic capabilities of existing enzyme platforms by exploiting new mechanistic paradigms. Photoenzymatic Hydrogenation of Heteroaromatic Olefins using 'Ene'-Reductases with Photoredox Catalysts.,Hyster T, Nakano Y, Black MJ, Meichan AJ, Sandoval BA, Chung M, Biegasiewicz K, Zhu T Angew Chem Int Ed Engl. 2020 Mar 17. doi: 10.1002/anie.202003125. PMID:32181943[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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