The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase.

@article{Grubmeyer1981ThePO,
  title={The presence of two hydrolytic sites on beef heart mitochondrial adenosine triphosphatase.},
  author={C Grubmeyer and Harvey S. Penefsky},
  journal={The Journal of biological chemistry},
  year={1981},
  volume={256 8},
  pages={3718-27}
}
The ribose-modified nucleotides 2',3'-O-(2,4,6-trinitrophenyl) adenosine 5'-triphosphate (TNP-ATP) and TNP-ADP were used to probe the catalytic sites on soluble beef heart mitochondrial adenosine triphosphatase (F1). Both compounds were potent competitive inhibitors of ATP hydrolysis catalyzed by F1, Ki = 5.5 and 10 nM, respectively, and by submitochondrial particles, Ki (TNP-ATP) = 21 nM. Both compounds also were potent competitive inhibitors of ATP synthesis during oxidative phosphorylation… CONTINUE READING

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