Hoe S T, Crabbe M J
Exp Eye Res. 1987 May;44(5):663-75. doi: 10.1016/s0014-4835(87)80137-9.
The chelating agents 1,10-phenanthroline and 2,2'-dipyridyl gave partial inhibition of the bovine lens aldehyde dehydrogenase, which was fully reversible and competitive towards acetaldehyde. The non-chelating compounds, 1,7-phenanthroline, 4,7-phenanthroline and 4,4'-dipyridyl gave total competitive inhibition, and significant activation at saturating substrate and coenzyme concentrations, in a manner similar to cyanide. All five isomers prevented the binding of the coenzyme NAD+, the non-chelating phenanthroline compounds being the most effective. An overall mechanism for inhibition by single and bidentate ligands is proposed.
螯合剂1,10 - 菲咯啉和2,2'-联吡啶对牛晶状体醛脱氢酶有部分抑制作用,这种抑制作用是完全可逆的,且对乙醛具有竞争性。非螯合化合物1,7 - 菲咯啉、4,7 - 菲咯啉和4,4'-联吡啶产生完全竞争性抑制,并在底物和辅酶浓度饱和时具有显著激活作用,其方式类似于氰化物。所有这五种异构体都能阻止辅酶NAD⁺的结合,其中非螯合菲咯啉化合物最为有效。本文提出了单齿和双齿配体抑制作用的总体机制。