Interaction of carbonyl cyanide 3-chlorophenylhydrazone with cytochrome c oxidase.
Cytochrome c oxidase binds protonophore carbonyl cyanide 3-chlorophenylhydrazone (CCCP) with high affinity. There are 1.46 high-affinity binding sites per cytochrome c oxidase for CCCP with dissociation constant 2.7 x 10(-7) mol/l. The bond between the CCCP and cytochrome c oxidase accomplishes through the group on cytochrome c oxidase with pKa 6.64 and is based on the electrostatic interaction. Interaction of CCCP with low-affinity binding sites of cytochrome c oxidase induces the shift of the anion CCCP spectrum to UV-region. The similar effect is characteristic for CCCP interaction with protons. Lipophilic non-dissociated derivative NCH3CCP is not binding to cytochrome c oxidase.
Bona
M
M
Department of Biophysics, Slovak Academy of Sciences, Kosice.
Antalík
M
M
Gazová
Z
Z
Kuchár
A
A
Dadák
V
V
Podhradský
D
D
D001665:Binding Sites; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone / Q000031:analogs & derivatives / Q000378:metabolism*; D003576:Electron Transport Complex IV / Q000378:metabolism*; D011485:Protein Binding
C089132:4-chlorophenyl-N-methylhydrazonopropanedinitrile; D002258:Carbonyl Cyanide m-Chlorophenyl Hydrazone; D003576:Electron Transport Complex IV