   1.2.5.3 | more |
metal cluster composition, structure and function of CO dehydrogenase synthesized in mutants of Oligotropha carboxidovorans strain OM5 in which the genes coxE, coxF and coxG are disrupted by insertional mutagenesis, recombinant expression in Escherichia coli strain S17-1, overview. Mutants in coxG retain the ability to utilize CO, although at a lower growth rate. They contain a regular CO dehydrogenase with a functional catalytic site. The CoxD protein is a distinct AAA+ ATPase. CoxD operates in the maturation of the CO dehydrogenase bimetallic cluster, particularly in the sulfuration of the [MoO3]-site and in ATP-dependent chaperone function. Disruption of coxD leads to a phenotype of D-km which is impaired in the utilization of CO, whereas the utilization of H2 plus CO2 is not affected. Under appropriate induction conditions, bacteria synthesize a fully assembled apo-CO dehydrogenase, which cannot oxidize CO. Apo-CO dehydrogenase contained a [MoO3] site in place of the [CuSMoO2] clusters. The genes coxE and coxF are both obligatory for the utilization of CO as a growth substrate |
736513 |
