Conferment of CO-Controlled Dimer–Monomer Transition Property to Thermostable Cytochrome <i>c</i>′ by Mutation in the Subunit–Subunit Interface

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  • Conferment of CO-Controlled Dimer?Monomer Transition Property to Thermostable Cytochrome c′ by Mutation in the Subunit?Subunit Interface

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Cytochrome c′ (CP) is a gas-binding homo-dimeric heme protein. Mesophilic Allochromatium vinosum CP (AVCP) and thermophilic Hydrogenophilus thermoluteolus CP (PHCP) have high sequence and structure similarities. AVCP is known to exhibit a dimer?monomer transition upon CO binding/dissociation, whereas detailed CO-binding properties of PHCP remain unrevealed. Here, we found that the CO-binding affinity of wild-type PHCP is lower than that of AVCP, and the PHCP dimer does not dissociate to monomers under CO-saturated reduced conditions. The CO-binding affinity of PHCP increased by mutations in the subunit?subunit interface (F11T, T18F, or F71D). The T18F, F71D, and T18F/F71D PHCP variants exhibited similar dimer?monomer transitions upon CO binding/dissociation to that of AVCP, although the F11T variant did not. The simulated structures of the PHCP variants revealed that the T18F and F71D mutations caused rearrangement in the subunit?subunit interface, whereas the F11T mutation did not, indicating that the effective dimer?monomer transitions upon CO binding/dissociation are induced by the rearrangement in the subunit?subunit interface. The present results indicate that subunit?subunit interface mutation of oligomeric proteins is a useful approach in the adjustment of protein stability and ligand binding affinity, leading to a change in the quaternary structure.

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