1zxi

<table><tr><td colspan='2'>[[1zxi]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Olico Olico]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZXI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZXI FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=CUM:CU(I)-S-MO(VI)(=O)OH+CLUSTER'>CUM</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=MCN:PTERIN+CYTOSINE+DINUCLEOTIDE'>MCN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Carbon-monoxide_dehydrogenase_(acceptor) Carbon-monoxide dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.99.2 1.2.99.2] </span></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=1zxi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zxi OCA], [http://pdbe.org/1zxi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zxi RCSB], [http://www.ebi.ac.uk/pdbsum/1zxi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zxi ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/DCMS_OLICO DCMS_OLICO]] Catalyzes the oxidation of carbon monoxide to carbon dioxide. [[http://www.uniprot.org/uniprot/DCMM_OLICO DCMM_OLICO]] Catalyzes the oxidation of carbon monoxide to carbon dioxide. [[http://www.uniprot.org/uniprot/DCML_OLICO DCML_OLICO]] Catalyzes the oxidation of carbon monoxide to carbon dioxide.

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== Publication Abstract from PubMed ==

Carbon monoxide dehydrogenase from the bacterium Oligotropha carboxidovorans catalyzes the oxidation of CO to CO(2) at a unique [CuSMoO(2)] cluster. In the bacteria the cluster is assembled post-translational. The integration of S, and particularly of Cu, is rate limiting in vivo, which leads to CO dehydrogenase preparations containing the mature and fully functional enzyme along with forms of the enzyme deficient in one or both of these elements. The active sites of mature and immature forms of CO dehydrogenase were converted into a [MoO(3)] centre by treatment with potassium cyanide. We have established a method, which rescues 50% of the CO dehydrogenase activity by in vitro reconstitution of the active site through the supply of sulphide first and subsequently of Cu(I) under reducing conditions. Immature forms of CO dehydrogenase isolated from the bacterium, which were deficient in S and/or Cu at the active site, were similarly activated. X-ray crystallography and electron paramagnetic resonance spectroscopy indicated that the [CuSMoO(2)] cluster was properly reconstructed. However, reconstituted CO dehydrogenase contains mature along with immature forms. The chemical reactions of the reconstitution of CO dehydrogenase are summarized in a model, which assumes resulphuration of the Mo-ion at both equatorial positions at a 1:1 molar ratio. One equatorial Mo-S group reacts with Cu(I) in a productive fashion yielding a mature, functional [CuSMoO(2)] cluster. The other Mo-S group reacts with Cu(I), then Cu(2)S is released and an oxo group is introduced from water, yielding an inactive [MoO(3)] centre.

Structural and functional reconstruction in situ of the [CuSMoO2] active site of carbon monoxide dehydrogenase from the carbon monoxide oxidizing eubacterium Oligotropha carboxidovorans.,Resch M, Dobbek H, Meyer O J Biol Inorg Chem. 2005 Aug;10(5):518-28. Epub 2005 Sep 23. PMID:16091936<ref>PMID:16091936</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1zxi" style="background-color:#fffaf0;"></div>

[[Category: Dobbek, H]]

[[Category: Meyer, O]]

[[Category: Resch, M]]

[[Category: Oxidoreductase]]