J. Biol. Chem., Vol. 262, Issue 21, 10077-10079, Jul, 1987
Reconstitution of monomeric cytochrome c oxidase into phospholipid vesicles yields functionally interacting cytochrome aa3 units
G Antonini, M Brunori, F Malatesta, P Sarti and MT Wilson
When the carbon monoxide complex of fully reduced cytochrome c oxidase,
reconstituted into liposomes, is mixed with oxygen-containing buffer,
complex kinetic progress curves are observed. This pattern is seen
irrespective of whether the oxidase used in reconstitution is the dimeric
or monomeric (subunit III-depleted) enzyme. These findings are interpreted
in the light of similar experiments on the detergent- solubilized enzyme
reported by Gibson and Greenwood (Gibson, Q.H., and Greenwood, C. (1963)
Biochem. J. 86, 541-554) and confirmed by ourselves. We conclude that
reconstitution of monomeric (subunit III- less) enzyme yields,
preferentially, vesicles containing more than one functional unit, possibly
associated as dimers. This result is of significance to our understanding
of the relationships between aggregation state and proton pumping capacity
of cytochrome oxidase.
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