两种不同四级结构的脱氧血红蛋白之间Fe(II)-Nε(组氨酸-F8)伸缩频率的差异。
Differences in Fe(II)-N epsilon(His-F8) stretching frequencies between deoxyhemoglobins in the two alternative quaternary structures.
作者信息
Nagai K, Kitagawa T
出版信息
Proc Natl Acad Sci U S A. 1980 Apr;77(4):2033-7. doi: 10.1073/pnas.77.4.2033.
Abstract
Resonance Raman spectra have been obtained of the alpha deoxy and beta deoxy subunits within valency hybrid hemoglobins both in the high-affinity (R) and low-affinity (T) structures. Upon conversion from the R to the T structure, the vibrational frequency of the Fe(II)-N epsilon(His-F8) bond changes from 223 to 207 or 203 cm-1 in the alpha deoxy subunit and from 224 to 220 or 217 cm-1 in the beta deoxy subunit. We estimate that the Fe(II)-N epsilon(His-F8) bond is stretched by the R leads to T transition 3 times more in the alpha subunit (0.024 A) than in the beta subunit (0.0085 A) and, accordingly, the strain energy developed in that bond is 8 times larger in the alpha than in the beta subunit. Hence, the oxygen affinity of the alpha and beta subunits may be regulated by different mechanisms.
摘要
已获得价态杂合血红蛋白中高亲和力（R）和低亲和力（T）结构下α-脱氧和β-脱氧亚基的共振拉曼光谱。从R结构转变为T结构时，α-脱氧亚基中Fe（II）-Nε（His-F8）键的振动频率从223变为207或203 cm-1，β-脱氧亚基中则从224变为220或217 cm-1。我们估计，R向T转变时，α亚基中Fe（II）-Nε（His-F8）键的拉伸程度（0.024 Å）是β亚基（0.0085 Å）的3倍，因此，该键中产生的应变能在α亚基中比在β亚基中大8倍。因此，α和β亚基的氧亲和力可能受不同机制调节。
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