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用人血红蛋白(HbA)和HbC首次制备了α_1 99 Lys-α_2 99 Lys交联的Fe(Ⅱ)-Co(Ⅱ)杂化血红蛋白:[α(Fe)β(Co)]_A[α(Co)β(Co)]_CXL,[α(Co)β(Fe)]_A[α(Co)·β(Co)]_CXL等。在500 MHz ~1H NMR和EPR谱仪上研究了它们在载氧、去氧和一氧化碳(CO)配位(无IHP或有IHP存在)时的三级和四级结构的变化。由样品的~1HNMR谱的T态和R态标志峰的变化,证明了在氧的配位过程中,氧分子首先结合在α(Fe)亚基上,而不是β(Fe)亚基上。实验结果还表明Hb在吸氧过程中,除了T态和R态之外,还存在一些中间过渡态,IHP的加入大大有利于从R态转向T态。77 K下的EPR谱的结果同样证实了这一点。
Α (Fe) β (Co)] _A [α (Co) β] was synthesized by using human hemoglobin (HbA) and HbC for the first time. (Co)] _ CXL, [α (Co) β (Fe)] _ A [α (Co) · β (Co)] _ CXL and the like. Their tertiary and quaternary structure changes were studied at 500 MHz ~ 1 H NMR and EPR spectroscopy in the presence of oxygen, deoxygenation and carbon monoxide (CO) coordination (no IHP or presence of IHP). The change of the T state and the R state sign of the ~ 1H NMR spectrum of the sample proves that the oxygen molecules are firstly bound to the α (Fe) subunit instead of the β (Fe) subunit during the coordination of oxygen. The experimental results also show that in addition to the T state and the R state, Hb in the oxygen absorption process, there are still some intermediate transition state, the addition of IHP greatly facilitates the transition from R state to T state. The EPR spectrum at 77 K also confirms this.