Abstract
Thiobacillus novellus cytochrome c oxidase has one heme a molecule and one copper atom in the minimal structural unit consisting of one molecule each of two subunits (32 and 23 kDa). The oxidase occurs as a monomer of the unit in the presence of 0.5% n-octyl-β-D-thioglucoside and as a dimer of the unit in the presence of 0.5% Tween 20. The heme molecule in the monomer is completely reactive with CO, that is, the monomeric oxidase appears to be cytochrome a3, while one of the two heure molecules in the dimer reacts with CO, that is, the dimeric oxidase appears to be cytochrome aa3. The [s]-v curve in the oxidation of ferrocytochrome c catalyzed by the dimeric oxidase is sigmoidal. On addition of ATP, the molecular mass of the dimeric oxidase becomes half and the [s]-v curve changes to a hyperbola from a sigmoid. Thus, ATP regulates the molecular states and catalytic properties of the oxidase.
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