M. Bona et al., INTERACTION OF CARBONYL CYANIDE 3-CHLOROPHENYLHYDRAZONE WITH CYTOCHROME-C-OXIDASE, General physiology and biophysics, 12(6), 1993, pp. 533-542
Cytochrome c oxidase binds protonophore carbonyl cyanide 3-chloropheny
lhydrazone (CCP) with high affinity. There are 1.46 high-affinity bind
ing sites per cytochrome c oxidase for CCCP with dissociation constant
2.7. 10(-7) mol/l. The bond between the CCCP and cytochrome c oxidase
accomplishes through the group on cytochrome c oxidase with pK(a), 6.
64 and is based on the electrostatic interaction. Interaction of CCCP
with low-affinity binding sites of cytochrome c oxidase induces the sh
ift of the anion CCCP spectrum to UV-region. The similar effect is cha
racteristic for CCCP interaction with protons. Lipophilic non-dissocia
ted derivative NCH3CCP is not binding to cytochrome c oxidase.