9f5u: Difference between revisions
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==Crystal structure of Heme-Oxygenase from Corynebacterium diphtheriae complexed with Cobalt-porphyrine (HumO-Co(III))== | |||
<StructureSection load='9f5u' size='340' side='right'caption='[[9f5u]], [[Resolution|resolution]] 1.15Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9f5u]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Corynebacterium_diphtheriae Corynebacterium diphtheriae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9F5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9F5U 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]] 1.15Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=9f5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9f5u OCA], [https://pdbe.org/9f5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9f5u RCSB], [https://www.ebi.ac.uk/pdbsum/9f5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9f5u ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q54AI1_CORDP Q54AI1_CORDP] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Light-dependent reduction of carbon dioxide (CO(2)) into value-added products can be catalyzed by a variety of molecular complexes. Here we report a rare example of a structurally characterized artificial enzyme, resulting from the combination of a heme binding protein, heme oxygenase, with cobalt-protoporphyrin IX, with good activity for the photoreduction of CO(2) to carbon monoxide (CO). Using a copper-based photosensitizer, thus making the photosystem free of noble metals, a large turnover frequency value of approximately 616 h(-1), a turnover value of approximately 589, after 3 h reaction, and a CO vs H(2) selectivity of 72% were obtained, establishing a record among previously reported artificial CO(2) reductases. Thorough photophysical studies allowed tracking of reaction intermediates and provided insights into the reaction mechanism. Thanks to a high-resolution crystal structure of the artificial enzyme, both in the absence and in the presence of the protein-bound CO(2) substrate, a rational site-directed mutagenesis approach was used to study the effect of some modifications of the active site on the activity. | |||
Light-Activated Artificial CO(2)-Reductase: Structure and Activity.,Labidi RJ, Faivre B, Carpentier P, Perard J, Gotico P, Li Y, Atta M, Fontecave M J Am Chem Soc. 2024 Oct 1. doi: 10.1021/jacs.4c08927. PMID:39352411<ref>PMID:39352411</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 9f5u" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Corynebacterium diphtheriae]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Atta M]] | ||
[[Category: Carpentier P]] | |||
[[Category: Faivre B]] | |||
[[Category: Fontecave M]] | |||
[[Category: Gotico P]] | |||
[[Category: Labidi RJ]] | |||
[[Category: Li Y]] | |||
[[Category: Perard J]] | |||