Coppey M, Tourbez H, Valat P, Alpert B
Nature. 1980 Apr 10;284(5756):568-70. doi: 10.1038/284568a0.
It is well known that the oxygen affinity of haemoglobin depends on the number of combined oxygen molecules. This cooperative effect is considered to arise from a reversible protein transition between two forms which differ in tertiary and quaternary structure. However, the various steps of the structural changes concerning the protein and the haem have not been identified. Using time-resolved spectroscopy coupled to flash photolysis, we have attempted to elucidate the influence of protein on the relaxation processes of haem in haemoglobin. We now report our first results obtained in a picosecond time-resolved resonance Raman study of haemoglobin.
众所周知，血红蛋白对氧气的亲和力取决于结合的氧分子数量。这种协同效应被认为源于两种形式之间可逆的蛋白质转变，这两种形式在三级和四级结构上有所不同。然而，与蛋白质和血红素相关的结构变化的各个步骤尚未明确。利用与闪光光解相结合的时间分辨光谱技术，我们试图阐明蛋白质对血红蛋白中血红素弛豫过程的影响。我们现在报告在血红蛋白的皮秒时间分辨共振拉曼研究中获得的首个结果。
