9gyb: Difference between revisions
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The | ==Crystal structure of the recombinant CODH from Rhodopspirillum rubrum produced in Escherichia coli== | ||
<StructureSection load='9gyb' size='340' side='right'caption='[[9gyb]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[9gyb]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodospirillum_rubrum Rhodospirillum rubrum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9GYB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9GYB 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]] 2.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=9gyb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9gyb OCA], [https://pdbe.org/9gyb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9gyb RCSB], [https://www.ebi.ac.uk/pdbsum/9gyb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9gyb ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/COOS_RHORU COOS_RHORU] Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The [NiFe]-CODH from Rhodospirillum rubrum contains [4Fe4S] clusters that allow electron transfer from the buried active sites to the protein surface. Among them, the role of the D-cluster, located at the dimer interface is still not fully understood. In this study, the removal of the D-cluster by site-directed mutagenesis revealed remarkable features in the behavior of the enzyme. Quantitative analysis and spectroscopic studies unveiled the suppression of D-cluster in the mutants and the influence on other metal cofactors. Furthermore, the CO oxidation activity in solution measured in the presence of methylviologen is almost completely abolished in the mutants. Conversely, direct electrochemistry at a functionalized carbon nanotube electrode shows that the mutants are still catalytically active reaching reduced but significant current densities of 0.7 mA cm(-2). Moreover, the electroenzymatic activity towards oxygen is not affected by the removal of the D cluster. EPR studies reveal a remarkable change in the magnetic coupling between FeS clusters upon removal of the D-cluster, highlighting the effect of the location of this D-cluster at the dimer interface. It is noteworthy that in addition to its role as electron relay, the D-cluster appears to play an important role in the biosynthesis of the active site. | |||
Insights into the Role of the D-Cluster in [NiFe]-CODH from Rhodospirillum Rubrum.,Contaldo U, Guigliarelli B, Perard J, Pichon T, Le Goff A, Cavazza C Chemistry. 2025 Feb 6:e202403648. doi: 10.1002/chem.202403648. PMID:39912726<ref>PMID:39912726</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Cavazza | <div class="pdbe-citations 9gyb" style="background-color:#fffaf0;"></div> | ||
[[Category: Contaldo | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Rhodospirillum rubrum]] | |||
[[Category: Cavazza C]] | |||
[[Category: Contaldo U]] | |||
Latest revision as of 17:56, 19 February 2025
Crystal structure of the recombinant CODH from Rhodopspirillum rubrum produced in Escherichia coliCrystal structure of the recombinant CODH from Rhodopspirillum rubrum produced in Escherichia coli
Structural highlights
FunctionCOOS_RHORU Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH). Publication Abstract from PubMedThe [NiFe]-CODH from Rhodospirillum rubrum contains [4Fe4S] clusters that allow electron transfer from the buried active sites to the protein surface. Among them, the role of the D-cluster, located at the dimer interface is still not fully understood. In this study, the removal of the D-cluster by site-directed mutagenesis revealed remarkable features in the behavior of the enzyme. Quantitative analysis and spectroscopic studies unveiled the suppression of D-cluster in the mutants and the influence on other metal cofactors. Furthermore, the CO oxidation activity in solution measured in the presence of methylviologen is almost completely abolished in the mutants. Conversely, direct electrochemistry at a functionalized carbon nanotube electrode shows that the mutants are still catalytically active reaching reduced but significant current densities of 0.7 mA cm(-2). Moreover, the electroenzymatic activity towards oxygen is not affected by the removal of the D cluster. EPR studies reveal a remarkable change in the magnetic coupling between FeS clusters upon removal of the D-cluster, highlighting the effect of the location of this D-cluster at the dimer interface. It is noteworthy that in addition to its role as electron relay, the D-cluster appears to play an important role in the biosynthesis of the active site. Insights into the Role of the D-Cluster in [NiFe]-CODH from Rhodospirillum Rubrum.,Contaldo U, Guigliarelli B, Perard J, Pichon T, Le Goff A, Cavazza C Chemistry. 2025 Feb 6:e202403648. doi: 10.1002/chem.202403648. PMID:39912726[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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