Müller F, van Berkel W J, Steennis P J
Biochem Int. 1983 Jul;7(1):115-22.
The flavoprotein p-hydroxybenzoate hydroxylase is inhibited by adenosine nucleotides, Cibacron blue, phosphate ions and metal ion complexes. The inhibition of the enzyme is competitive with respect to NADPH. The most potent inhibitors of the enzyme are Cibacron blue and the metal ion complexes whereas the inhibition by the adenosine nucleotides is comparable to that by halogen ions. Some inhibitors cause quenching of the fluorescence emission of the protein-bound prosthetic group or perturb the absorption spectrum of the enzyme in the visible region allowing determination of the dissociation constant of the interaction between the free or the substrate-complexed enzyme and the inhibitors. The inhibition constants are in good agreement with the dissociation constants.
黄素蛋白对羟基苯甲酸羟化酶受到腺苷核苷酸、汽巴克隆蓝、磷酸离子和金属离子络合物的抑制。该酶的抑制作用相对于NADPH而言是竞争性的。该酶最有效的抑制剂是汽巴克隆蓝和金属离子络合物，而腺苷核苷酸的抑制作用与卤素离子的抑制作用相当。一些抑制剂会导致蛋白质结合辅基的荧光发射淬灭，或在可见光区域扰乱该酶的吸收光谱，从而可以测定游离或底物复合酶与抑制剂之间相互作用的解离常数。抑制常数与解离常数高度吻合。
