Spectroscopic and Chemical Probes for Coupled Binuclear Copper Protein Sites: RUI

拉拉比博士正在开发并使用三种不同的结构探针技术来研究血蓝蛋白、酪氨酸酶和漆酶中的偶联双核铜位。这些探针是：1)其他金属取代铜，然后进行UV/Vis，CD和MCD光谱研究；2)外源配体与天然和金属取代的蛋白质结合，然后进行光谱研究；3)结合外源配体的内振动模式的红外光谱研究。偶联双核铜存在于从真菌到人类的各种生命系统蛋白质的活性部位。这些蛋白质参与氧运输(血蓝蛋白)或氧的激活(酪氨酸、漆酶)。由于这些蛋白质的大小和复杂性，其活性部位的确切结构尚不清楚。我们对这些结构的大部分知识都是通过研究它们的光谱性质而发展起来的。

Dr. Larrabee is developing and using three different structural probe techniques to study the coupled binuclear copper sites in hemocyanin, tyrosinase and laccase. These probes are: 1) substitution of other metals for copper followed by uv/vis, CD and MCD spectral studies; 2) binding of exogenous ligands to the native and metal substituted proteins, followed by spectral studies, and 3) infrared spectroscopy of the internal vibrational modes of bound exogenous ligands. Coupled binuclear copper is found at the active site of a variety of proteins of living systems from fungi to humans. These proteins are involved in oxygen transport (hemocyanins) or in activation of dioxygen (tyrosine, laccase). Because of the large size and complexity of these proteins the exact structures of their active sites are unknown. Most of our knowledge of these structures has developed through the study of their spectroscopic properties.