View source for 9tox


==CO dehydrogenase 2 variant A559W==
<StructureSection load='9tox' size='340' side='right'caption='[[9tox]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9tox]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Carboxydothermus_hydrogenoformans_Z-2901 Carboxydothermus hydrogenoformans Z-2901]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9TOX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9TOX 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]] 1.49&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</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=9tox FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9tox OCA], [https://pdbe.org/9tox PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9tox RCSB], [https://www.ebi.ac.uk/pdbsum/9tox PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9tox ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/COOS2_CARHZ COOS2_CARHZ] CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH) (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In their recent communication in Angewandte Chemie (10.1002/anie.202508565), Suk Min Kim and coworkers have described the effect of modifying the gas channels of the CO dehydrogenase II from Carboxydothermus hydrogenoformans, an enzyme that oxidizes reversibly CO into CO(2). Their goal was to use mutagenesis to slow down the arrival of O(2) at the active site. They reported a large increase in the resistance against oxygen, one of the major barriers to the application of this extremely fast and efficient enzyme in biotechnological devices, with an increase in the IC(50) of more than two orders of magnitudes for some variants, with only a minor impact on the affinity of the enzyme for CO. We have produced the same variants, and characterized them in depth using Protein Film Electrochemistry. We used an approach that has proven very useful to learn and understand about the reactivity of CO dehydrogenases (and other redox enzymes like hydrogenases) with O(2). We found that, contrary to the claims by Kim and coworkers, the A559W and the A559W/V610H mutants are not more resistant than the wild type against oxygen.

Correspondence on "Fortification of FeS Clusters Reshapes Anaerobic CO Dehydrogenase Into an Air-Viable Enzyme Through Multilayered Sealing of O(2) Tunnels".,Opdam LV, Gebhardt P, Leger C, Dobbek H, Fourmond V Angew Chem Int Ed Engl. 2026 May 23:e1942100. doi: 10.1002/anie.1942100. PMID:42175862<ref>PMID:42175862</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9tox" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Carboxydothermus hydrogenoformans Z-2901]]
[[Category: Large Structures]]
[[Category: Dobbek H]]
[[Category: Gebhardt P]]
[[Category: Jeoung J-H]]