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Bioresources and Bioprocessing
Fig. 2 | Bioresources and Bioprocessing

Fig. 2

From: Current status of carbon monoxide dehydrogenases (CODH) and their potential for electrochemical applications

Fig. 2

Subunit and cluster composition of aerobic Mo,Cu-containing CODHs. Dimer of heterotrimers, where each heterotrimer is formed by a large subunit containing Mo,Cu active site (CoxL, white dot), a medium FAD containing flavoprotein subunit (CoxM) and a small iron–sulfur subunit (CoxS). FAD, flavo-adenin-dinucleotide; A and B, iron–sulfur–cluster [Fe2S2]. The crystal structure of the Mo/Cu-dependent CODH from Oligotropha carboxidovorans in its oxidized form is shown in the background (PDB ID:1N5W) (Dobbek et al. 2002). The graphical design of the crystal structure was performed with UCSF Chimera (Pettersen et al. 2004)

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