EC Number   |
Inhibitors |
Structure |
|---|
    7.1.1.9 | 4-hydroxynonenal |
time- and concentration-dependent inhibition of cytochrome c oxidase activity. Superoxide dismutase and catalase and the HO radical scavenger mannitol partially prevent inhibition of cytochrome c oxidase activity |
   |
| 7.1.1.9 | aluminium phosphite |
decrease in catalytic efficiency of active enzyme molecules on treatment with aluminium phosphide |
|
| 7.1.1.9 | amyloid beta |
native, up to 65% inhibition. Amyloid beta mutation Y10A does not affect maximal inhibition, but the altered peptide needs a longer period for ageing. Substitution M35V or oxidizing the sulfur of M35 to a sulfoxide completely abrogates the peptides inhibitory potential. Inhibition depends completely on presence of divalent Cu2+ and may involve the formation of a redox active amyloid-beta-methionine radical |
|
| 7.1.1.9 | amyloid beta1-42 |
synthetic peptide, dimeric amyloid beta specifically inhibits the cytochrome-c oxidase dependent on presence of Cu2+ and specific ageing of the amyloid beta1-42 solution |
|
| 7.1.1.9 | ATP |
the ATP-inhibition of CcO is only effective at very high ATP/ADP ratios (above 50) in the mitochondrial matrix or at low concentrations of ferrocytochrome c |
|
| 7.1.1.9 | ATP |
ATP inhibition occurs under uncoupled conditions (in the presence of carbonly cyanide m-chlorophenyl hydrazine) when the classical respiratory control is absent. High ATP/ADP ratios in the matrix as well as in the cytosolic space are required for full ATP inhibition of the enzyme |
|
| 7.1.1.9 | azide |
- |
|
| 7.1.1.9 | azide |
heme-binding inhibitor, noncompetitive vs. O2 and cytochrome c |
|
| 7.1.1.9 | azide |
0.08 mM, 50% inhibition |
|
| 7.1.1.9 | azide |
0.1 mM, 50% inhibition |
|
