Journal
JOURNAL OF BIOLOGICAL INORGANIC CHEMISTRY
Volume 23, Issue 4, Pages 613-620Publisher
SPRINGER
DOI: 10.1007/s00775-018-1541-0
Keywords
Carbon monoxide dehydrogenase; Active site; Iron-sulfur cluster; Maturation
Funding
- CNRS
- Aix Marseille Universite
- Agence Nationale de la Recherche [ANR-12-BS08-0014, ANR-14-CE05-0010, ANR-15-CE05-0020, ANR-17-CE11-0027]
- A*MIDEX Grant by the French Government Investissements d'Avenir program [ANR-11-IDEX-0001-02]
- Erasmus program
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Nickel-containing enzymes are diverse in terms of function and active site structure. In many cases, the biosynthesis of the active site depends on accessory proteins which transport and insert the Ni ion. We review and discuss the literature related to the maturation of carbon monoxide dehydrogenases (CODH) which bear a nickel-containing active site consisting of a [Ni-4Fe-4S] center called the C-cluster. The maturation of this center has been much less studied than that of other nickel-containing enzymes such as urease and NiFe hydrogenase. Several proteins present in certain CODH operons, including the nickel-binding proteins CooT and CooJ, still have unclear functions. We question the conception that the maturation of all CODH depends on the accessory protein CooC described as essential for nickel insertion into the active site. The available literature reveals biological variations in CODH active site biosynthesis.
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