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在生物学领域中,利用 CARS 光谱可以进一步研究生物分子结构及其和功能的关系等基本问题。(1)人或动物在 CO 中毒时,血液内生成一氧化碳血红蛋白(简写作 COHb)。COHb 易于光解。COHb 的 CARS 谱表明,COHb 未被光解时,预期在1589 cm~(-1)和1617-1642 cm~(-1)应有谱线出现。但在 CO 配位体光解后的6毫微秒内,CARS 谱内并没有出现这些谱线。由此推断,COHb 中的铁原子离开了血红素平面,到了其脱氧血红蛋白中的位置(位移0.60(?))。(2)黄素腺嘌呤二核甙酸(FAD)和葡萄糖氧化酶(前者是强荧光物质)的 CARS 光谱表明,FAD 束缚于葡萄糖氧化酶时,其1359 cm~(-1)谱带增加了12 cm~(-1)(变为1371 cm~(-1)),是由于 N_3质子和一个蛋白受体成了氢键引起的。(3)眼内视网膜上菌视紫质的 CARS 谱表明,暗适应菌视紫质的光谱和明适应菌视紫质的光谱是不同的。
In the field of biology, CARS spectroscopy can be used to further study the basic problems of biological molecular structure and its relationship with function. (1) When human or animal is poisoned by CO, carbon monoxide hemoglobin (abbreviated as COHb) is generated in the blood. COHb easy to photolytic. The CARS spectrum of COHb indicates that the expected spectral lines at 1589 cm -1 and 1617-1642 cm -1 should be expected when COHb is not photolysised. However, within 6 nanoseconds after CO ligand photolysis, these lines did not appear in the CARS spectrum. From this, we deduced that the iron atom in COHb left the heme plane and reached its deoxy-hemoglobin position (0.60 (?) Shift). (2) The CARS spectrum of flavin adenine dinucleotide (FAD) and glucose oxidase (the former is a strong fluorescent substance) showed that when FAD was bound to glucose oxidase, its 1359 cm -1 band increased 12 cm -1 (1371 cm -1) due to hydrogen bonding between the N 3 proton and one of the protein receptors. (3) The CARS spectrum of bacteriorhodopsin in intraocular retina showed that the spectrum of dark adapted rhodopsin was different from the spectrum of rhodopsin.