A minimum catalytic unit of F1‐ATPase shows non‐cooperative ATPase activity inherent in a single catalytic site with a Km 70 μM
Open Access
- 17 July 1995
- journal article
- Published by Wiley in FEBS Letters
- Vol. 368 (2) , 207-210
- https://doi.org/10.1016/0014-5793(95)00644-o
Abstract
F1‐ATPase has three interacting catalytic sites and shows complicated kinetics. Here, we report reconstitution of a complex, most likely composed of one α subunit and one β subunit, with a single catalytic site from thermophilic Bacillus PS3 F1‐ATPase on the solid surface. The complex has an ATPase activity which obeys a simple non‐cooperative kinetics with a K m(ATP) of 70 μM and a V max of 0.1 unit/mg. Different from F1‐ATPase, the complex is not inactivated by 7‐chrolo‐4‐nitrobenzofrazan. Thus, the inherent activity attributable to a single catalytic site unaffected by other catalytic sites of F1‐ATPase is characterized.Keywords
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