A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase.
A resonance Raman study of substrate and inhibitor binding to protocatechuate-3,4-dioxygenase.
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与原儿茶酸 3,4-双加氧酶结合的底物和抑制剂的共振拉曼研究。
DOI：
10.1016/0006-291x(78)91239-1
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发表时间：
1978
影响因子：
3.1
通讯作者：
S. W. May
中科院分区：
文献类型：
--
作者：
R. Felton;L. D. Cheung;R. Phillips;S. W. May
获得了原儿茶酸-3，4-双加氧酶与底物和羟基苯甲酸抑制剂复合物的共振拉曼光谱。这些数据建立金属配位这些结合的物种，并进一步表明，酪氨酸连接，存在于静息酶，不改变的配合物。对于抑制剂3-氯-4-羟基苯甲酸酯和3-氟-4-羟基苯甲酸酯，数据被解释为指示通过酚盐官能团的铁连接。对于底物，3，4-二羟基苯基丙酸，螯合通过theo-二羟基基团提出。在所有三种复合物中，存在于静息酶中的酪氨酸配体不被置换。利用抑制剂散射强度作为内标来估计两个酪氨酸在活性位点处与铁配位。
Resonance Raman spectra were obtained for complexes of protocatechuate-3,4-dioxygenase with substrate and hydroxybenzoate inhibitors. The data establish metal coordination by these bound species and demonstrate further that tyrosine ligation, present in the resting enzyme, is not altered in the complexes. For the inhibitors, 3-chloro-4-hydroxybenzoate and 3-fluoro-4-hydroxybenzoate, the data are interpreted as indicating iron ligation by the phenolate functionality. For the substrate, 3,4-dihydroxyphenylproprionate, chelation via theo-dihydroxy grouping is proposed. In all three complexes tyrosine ligands present in the resting enzyme are not displaced. The inhibitor scattering intensity was utilized as an internal standard to estimate that two tyrosines are coordinated to the iron at the active site.