Friedman J M, Rousseau D L, Ondrias M R, Stepnoski R A
Science. 1982 Dec 17;218(4578):1244-6. doi: 10.1126/science.7146910.
Low-frequency resonance Raman spectra of transient hemoglobin species were observed within 10 nanoseconds of photolysis. The Raman frequencies of the iron-proximal histidine stretching mode for transient species having either the R or the T quaternary structure are higher than in the corresponding deoxy species. The observed frequency difference in the iron-histidine mode between the R- and T- state transients indicates that there are quaternary structure-dependent protein forces on the iron-histidine bond in the liganded hemoglobins. These differences are interpreted in terms of changes in the tilt of the histidine with respect to the heme plane.
在光解后10纳秒内观测到了瞬态血红蛋白物种的低频共振拉曼光谱。具有R或T四级结构的瞬态物种的铁近端组氨酸伸缩模式的拉曼频率高于相应的脱氧物种。在R态和T态瞬态之间观察到的铁-组氨酸模式频率差异表明，在配体血红蛋白中，铁-组氨酸键上存在四级结构依赖性蛋白质作用力。这些差异可根据组氨酸相对于血红素平面的倾斜变化来解释。
