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Biochim Biophys Acta. 1994 Jun 28;1186(1-2):43-51.

ATP synthesis and hydrolysis of the ATP-synthase from Micrococcus luteus regulated by an inhibitor subunit and membrane energization.

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  • 1Institute of Biochemistry, Joh. Gutenberg-University, Mainz, Germany.


After incubation for 70 min in Tris-HCl (pH 8.0), the rate of ATP hydrolysis of free and reconstituted ATP-synthase from Micrococcus luteus multiplied about three times. The apparent increase in activity is due to the reversible dissociation of the delta-subunit. Results of experiments on the temperature dependence of the ATP hydrolysis rate of substrate saturated ATP-synthase exhibited a discontinuity in the Arrhenius plot at 32 +/- 0.5 degrees C for the delta-subunit associated enzyme. Below 32 +/- 0.5 degrees C the activation energy, Ea, was 231.5 +/- 5 kJ mol-1, while above this temperature-level it decreased to 76.4 +/- 3 kJ mol-1. ATP synthesis and hydrolysis of the ATP-synthase, co-reconstituted with monomeric bacteriorhodopsin (Halobacterium halobium), showed a lag of 50 s upon the illumination with green light (505-575 nm). This retardation and the activity depended on the ATP-synthase concentration, being typical of the dissociation of an inhibitor protein. The N-terminal protein sequences of the delta- and epsilon-subunit of the ATP-synthase were identified by automated Edman degradation. Alignment of the amino acid sequence and secondary structure calculations for the delta-subunit did not reveal homology to other known ATP-synthase delta-subunits, but significant equivalence to the epsilon-subunit of E. coli. Sequence analysis of the epsilon-subunit from M. luteus showed homology to equivalent regions in delta-subunits and Oligomycin Sensitivity Conferring Protein (OSCP) of other organisms.

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