Multifaceted effects of ATP on cardiolipin-bound cytochrome c Academic Article uri icon

abstract

  • Using a collection of dye-labeled cytochrome c (cyt c) variants, we identify transformations of the heterogeneous cardiolipin (CL)-bound cyt c ensemble with added ATP. Distributions of dye-to-heme distances P(r) from time-resolved fluorescence resonance energy transfer show that ATP decreases the population of largely unfolded cyt c conformers, but its effects are distinct from those of a simple salt. The high peroxidase activity of CL-bound cyt c with added ATP suggests binding interactions that favor protein structures with the open heme pocket. Although ATP weakens cyt c-CL binding interactions, it also boosts the apoptosis-relevant peroxidase activity of CL-bound cyt c.

authors

  • Snider, EJ
  • Muenzner, J
  • Toffey, JR
  • Hong, Y
  • Pletneva, EV

publication date

  • 2013