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- W802382155 abstract "Despite its toxicity CO can be used by several bacteria and archaea as a chemolithotrophic growth substrate, providing these microorganisms with energy and a carbon source [1]. CO dehydrogenases are the key enzymes in this process and catalyse the formal reaction: CO + H2O CO2 + 2H + + 2e . The crystals structures of CO dehydrogenases from aerobic and anaerobic bacteria revelaed unique active site architectures containing Cu, Mo, Fe, S and Ni [2-6]. The enzyme of the aerobic bacterium Oligotropha carboxidvorans revealed a binuclear active site in which Mo and Cu are bridged by sulfido-ligand [3]. The anaerobic bacterium Carboxydothermus hydrogenoformans employs for the same reaction an unrelated enzyme with an active site containing a [Ni-4Fe-5S] cluster [4]. Insight into the catalytic CO oxidation at these metal clusters has been gained by structural studies of different active and inhibited states of the enzymes [3-6]. Acetyl-CoA synthase (ACS) catalyses the synthesis of acetyl-CoA from CO, originating either from the environment or from the reduction of CO2 by a CO dehydrogenase, a methyl group, transferred by the corrinoid/iron-sulfur protein, and CoA. The active site of the monomeric enzyme from C. hydrogenoformans contains a Ni-Ni-[4Fe-4S] cluster [6]. Recent insights into structural details of the two reactions will be presented." @default.
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- W802382155 date "2003-03-01" @default.
- W802382155 modified "2023-09-23" @default.
- W802382155 title "Aerobic and anaerobic life on carbon monoxide" @default.
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