Bradley F C, Lindstedt S, Lipscomb J D, Que L, Roe A L, Rundgren M
J Biol Chem. 1986 Sep 5;261(25):11693-6.
A resonance Raman investigation into the blue chromophore of 4-hydroxyphenylpyruvate dioxygenase, a non-heme iron enzyme from Pseudomonas P. J. 874, reveals the presence of enhanced vibrations characteristic of tyrosinate coordination to the iron center. The excitation profiles for these features show that they are associated with the 595 nm absorption feature. EPR studies of this enzyme indicate the presence of a high-spin ferric center in a rhombic environment, as evidenced by a signal at g = 4.3 with the correct intensity for the measured iron content. This enzyme thus belongs to the emerging class of iron-tyrosinate proteins.
对来自假单胞菌P. J. 874的非血红素铁酶4-羟基苯丙酮酸双加氧酶的蓝色发色团进行的共振拉曼研究表明,存在酪氨酸盐与铁中心配位的增强振动特征。这些特征的激发谱表明它们与595 nm吸收特征相关。该酶的电子顺磁共振研究表明,在菱形环境中存在高自旋铁中心,g = 4.3处的信号证明了这一点,其强度与测得的铁含量相符。因此,这种酶属于新兴的铁-酪氨酸蛋白类别。