The photosynthetic F1-α 3β 3 and α 1β 1 catalytic core complexes.

Minimal photosynthetic catalytic F1(αβ) core complexes, containing equimolar ratios of the α and β subunits, were isolated from membrane-bound spinach chloroplast CF1 and Rhodospirillum rubrum chromatophore RrF1. A CF1-α3β3 hexamer and RrF1-α1β1 dimer, which were purified from the respective F1(αβ) complexes, exhibit lower rates and different properties from their parent F1-ATPases. Most interesting is their complete resistance to inhibition by the general F1 inhibitor azide and the specific CF1 inhibitor tentoxin. These inhibitors were earlier reported to inhibit multisite, but not unisite, catalysis in all sensitive F1-ATPases and were therefore suggested to block catalytic site cooperativity. The absence of this typical property of all F1-ATPases in the α1β1 dimer is consistant with the view that the dimer contains only a single catalytic site. The α3β3 hexamer contains however all F1 catalytic sites. Therefore the observation that CF1-α3β3 can bind tentoxin and is stimulated by it suggests that the F1γ subunit, which is required for obtaining inhibition by tentoxin as well as azide, plays an important role in the cooperative interactions between the F1-catalytic sites.