Waldo G S, Ling J, Sanders-Loehr J, Theil E C
Department of Biochemistry, North Carolina State University, Raleigh 27695.
Science. 1993 Feb 5;259(5096):796-8. doi: 10.1126/science.8430332.
An iron(III)-tyrosinate complex was identified in ferritin by ultraviolet-visible and resonance Raman spectroscopies. Previously, a specific amino acid side chain coordinated to iron in ferritin was not known. Ferritin protein was overexpressed in Escherichia coli from complementary DNA sequences of bullfrog red cell ferritin. The purple iron(III)-tyrosinate intermediate that formed during the first stages of iron uptake was replaced by the amber multinuclear iron(III)-oxo complexes of fully mineralized ferritin. Only the H subunit formed detectable amounts of the iron(III)-tyrosinate complex, which may explain the faster rates of iron biomineralization in H- compared to L-type ferritin.
通过紫外可见光谱和共振拉曼光谱在铁蛋白中鉴定出一种酪氨酸铁（III）配合物。此前，尚不清楚铁蛋白中与铁配位的特定氨基酸侧链。铁蛋白蛋白在大肠杆菌中由牛蛙红细胞铁蛋白的互补DNA序列过表达。在铁摄取的第一阶段形成的紫色酪氨酸铁（III）中间体被完全矿化的铁蛋白的琥珀色多核铁（III）-氧配合物所取代。只有H亚基形成了可检测量的酪氨酸铁（III）配合物，这可能解释了与L型铁蛋白相比，H型铁蛋白中铁生物矿化速率更快的原因。
