1SU7

Carbon Monoxide Dehydrogenase from Carboxydothermus hydrogenoformans- DTT reduced state

1SU7 の概要

• エントリーDOI: 10.2210/pdb1su7/pdb
• 関連するPDBエントリー: 1SU6 1SU8 1SUF
• 分子名称: Carbon monoxide dehydrogenase 2, IRON/SULFUR CLUSTER, FE2/S2 (INORGANIC) CLUSTER, ... (5 entities in total)
• 機能のキーワード: codh, carbon monoxide dehydrogenase, nickel, cluster c, oxidoreductase
• 由来する生物種: Carboxydothermus hydrogenoformans
• 細胞内の位置: Cytoplasm : Q9F8A8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 67962.34

構造登録者

Dobbek, H.,Svetlitchnyi, V.,Liss, J.,Meyer, O. (登録日: 2004-03-26, 公開日: 2004-05-11, 最終更新日: 2024-02-14)

主引用文献

Dobbek, H.,Svetlitchnyi, V.,Liss, J.,Meyer, O.
Carbon Monoxide Induced Decomposition of the Active Site [Ni-4Fe-5S] Cluster of CO Dehydrogenase
J.Am.Chem.Soc., 126:5382-5387, 2004

PubMed Abstract: 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.

PubMed: 15113209
DOI: 10.1021/ja037776v

実験手法

X-RAY DIFFRACTION (1.12 Å)