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| | {{STRUCTURE_1su7| PDB=1su7 | SCENE= }} | | {{STRUCTURE_1su7| PDB=1su7 | SCENE= }} |
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| - | '''Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans- DTT reduced state'''
| + | ===Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans- DTT reduced state=== |
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| - | ==Overview==
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| - | During the past two years, crystal structures of Cu- and Mo-containing carbon monoxide dehydrogenases (CODHs) and Ni- and Fe-containing CODHs have been reported. The active site of CODHs from anaerobic bacteria (cluster C) is composed of Ni, Fe, and S for which crystallographic studies of the enzymes from Carboxydothermus hydrogenoformans, Rhodospirillum rubrum, and Moorella thermoaceticarevealed structural similarities in the overall protein fold but showed substantial differences in the essential Ni coordination environment. The [Ni-4Fe-5S] cluster C in the fully catalytically competent dithionite-reduced CODH II from C. hydrogenoformans (CODHII(Ch)) at 1.6 A resolution contains a characteristic mu(2)-sulfido ligand between Ni and Fe1, resulting in a square-planar ligand arrangement with four S-ligands at the Ni ion. In contrast, the [Ni-4Fe-4S] clusters C in CO-treated CODH from R. rubrum resolved at 2.8 A and in CO-treated acetyl-CoA synthase/CODH complex from M. thermoacetica at 2.2 and 1.9 A resolution, respectively, do not contain the mu(2)-sulfido ligand between Ni and Fe1 and display dissimilar geometries at the Ni ion. The [Ni-4Fe-4S] cluster is composed of a cubane [Ni-3Fe-4S] cluster linked to a mononuclear Fe site. The described coordination geometries of the Ni ion in the [Ni-4Fe-4S] cluster of R. rubrum and M. thermoacetica deviate from the square-planar ligand geometry in the [Ni-4Fe-5S] cluster C of CODHII(Ch). In addition, the latter was converted into a [Ni-4Fe-4S] cluster under specific conditions. The objective of this study was to elucidate the relationship between the structure of cluster C in CODHII(Ch) and the functionality of the protein. We have determined the CO oxidation activity of CODHII(Ch) under different conditions of crystallization, prepared crystals of the enzyme in the presence of dithiothreitol or dithionite as reducing agents under an atmosphere of N(2) or CO, and solved the corresponding structures at 1.1 to 1.6 A resolutions. Fully active CODHII(Ch) obtained after incubation of the enzyme with dithionite under N(2) revealed the [Ni-4Fe-5S] cluster. Short treatment of the enzyme with CO in the presence of dithiothreitol resulted in a catalytically competent CODHII(Ch) with a CO-reduced [Ni-4Fe-5S] cluster, but a prolonged treatment with CO caused the loss of CO-oxidizing activity and revealed a [Ni-4Fe-4S] cluster, which did not contain a mu(2)-S. These data suggest that the [Ni-4Fe-4S] cluster of CODHII(Ch) is an inactivated decomposition product originating from the [Ni-4Fe-5S] cluster.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15113209}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15113209 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15113209}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Codh]] | | [[Category: Codh]] |
| | [[Category: Nickel]] | | [[Category: Nickel]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:08:23 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:57:02 2008'' |
Revision as of 12:57, 27 July 2008
Template:STRUCTURE 1su7
Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans- DTT reduced state
Template:ABSTRACT PUBMED 15113209
About this Structure
1SU7 is a Single protein structure of sequence from Carboxydothermus hydrogenoformans. Full crystallographic information is available from OCA.
Reference
Carbon monoxide induced decomposition of the active site [Ni-4Fe-5S] cluster of CO dehydrogenase., Dobbek H, Svetlitchnyi V, Liss J, Meyer O, J Am Chem Soc. 2004 May 5;126(17):5382-7. PMID:15113209
Page seeded by OCA on Sun Jul 27 15:57:02 2008
