6T7J

As-isolated Ni-free crystal structure of carbon monoxide dehydrogenase from Thermococcus sp. AM4 produced without CooC maturase

6T7J の概要

• エントリーDOI: 10.2210/pdb6t7j/pdb
• 分子名称: Carbon monoxide dehydrogenase, IRON/SULFUR CLUSTER, FE2/S2 (INORGANIC) CLUSTER, ... (9 entities in total)
• 機能のキーワード: ni-free cluster c, co dehydrogenase, oxidoreductase
• 由来する生物種: Thermococcus sp. AM4
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 208091.01

構造登録者

Dobbek, H.,Jeoung, J.-H. (登録日: 2019-10-22, 公開日: 2020-11-18, 最終更新日: 2024-01-24)

主引用文献

Benvenuti, M.,Meneghello, M.,Guendon, C.,Jacq-Bailly, A.,Jeoung, J.H.,Dobbek, H.,Leger, C.,Fourmond, V.,Dementin, S.
The two CO-dehydrogenases of Thermococcus sp. AM4.
Biochim Biophys Acta Bioenerg, 1861:148188-148188, 2020

PubMed Abstract: Ni-containing CO-dehydrogenases (CODHs) allow some microorganisms to couple ATP synthesis to CO oxidation, or to use either CO or CO as a source of carbon. The recent detailed characterizations of some of them have evidenced a great diversity in terms of catalytic properties and resistance to O. In an effort to increase the number of available CODHs, we have heterologously produced in Desulfovibrio fructosovorans, purified and characterized the two CooS-type CODHs (CooS1 and CooS2) from the hyperthermophilic archaeon Thermococcus sp. AM4 (Tc). We have also crystallized CooS2, which is coupled in vivo to a hydrogenase. CooS1 and CooS2 are homodimers, and harbour five metalloclusters: two [Ni4Fe-4S] C clusters, two [4Fe-4S] B clusters and one interfacial [4Fe-4S] D cluster. We show that both are dependent on a maturase, CooC1 or CooC2, which is interchangeable. The homologous protein CooC3 does not allow Ni insertion in either CooS. The two CODHs from Tc have similar properties: they can both oxidize and produce CO. The Michaelis constants (K) are in the microM range for CO and in the mM range (CODH 1) or above (CODH 2) for CO. Product inhibition is observed only for CO reduction, consistent with CO binding being much weaker than CO binding. The two enzymes are rather O sensitive (similarly to CODH II from Carboxydothermus hydrogenoformans), and react more slowly with O than any other CODH for which these data are available.

PubMed: 32209322
DOI: 10.1016/j.bbabio.2020.148188

実験手法

X-RAY DIFFRACTION (2.43 Å)