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Literature summary for 1.2.7.4 extracted from

  • Spangler, N.J.; Lindahl, P.A.; Bandarian, V.; Ludden, P.W.
    Spectroelectrochemical characterization of the metal centers in carbon monoxide dehydrogenase (CODH) and nickel-deficient CODH from Rhodospirillum rubrum (1996), J. Biol. Chem., 271, 7973-7977.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Iron the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [Fe4S4]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor Rhodospirillum rubrum
Nickel the enzyme contains two metal centers: a Ni-X-[4Fe-4S]2+/1+ cluster, i.e. C-center, that serves as the CO-oxidation site and a standard [4Fe-4S]2+/1+ cluster, i.e. B-center, that mediates electron flow from the C-center to the external electron acceptor, the nickel cation is proposed to be Ni2+ of the oxidized state of the C-center and in the one-electron-reduced state of the C-center, appears to strongly affect the redox behavior of the [4Fe-4S]2+/1+ component of the C-center Rhodospirillum rubrum

Organism

Organism UniProt Comment Textmining
Rhodospirillum rubrum
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