Related Experiment Videos
Properties and regulation of the H+-ATP synthase of mitochondria
O B Martins1, A Gómez-Puyou, M Tuena de Gómez-Puyou
1Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, México City.
Biophysical Chemistry
|February 1, 1988
Abstract:
A brief survey is made of the function of the H+-ATP synthase of mitochondria with emphasis on how it is regulated. A main regulatory factor is a low molecular weight protein whose binding to the enzyme appears to be essential for optimal accumulation of ATP as driven by electron transport. The ATP synthase is also controlled by ADP that, by binding to a site in the enzyme, inhibits ATP hydrolysis. Data on the spontaneous synthesis of a tightly bound ATP are discussed. Apparently, this requires proper subunit interactions to yield a competent catalytic site.