Intermediate spin‐states in one‐electron reduction of oxygen—hemoprotein complexes at low temperature
Intermediate spin‐states in one‐electron reduction of oxygen—hemoprotein complexes at low temperature
复制标题
低温氧-血红素复合物单电子还原的中间自旋态
DOI：
10.1016/0014-5793(79)80730-9
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发表时间：
1979
期刊：
影响因子：
3.5
通讯作者：
Zbigniew Gasyna
中科院分区：
文献类型：
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作者：
Zbigniew Gasyna
氧-血红素蛋白复合物的氧-血红素单位含有超过亚铁态的四个氧化当量。因此，氧血红素中心的一个电子当量还原将使其正式转化为t5的氧化态。已知该氧化态代表过氧化物酶的催化中间体化合物I [1，2]。然而，在氧储存和运输血红素蛋白如肌红蛋白和血红蛋白的情况下，没有发现这样的中间化合物。这些结果似乎与血红素蛋白和酶的氧合血红素复合物的催化特异性和反应性的差异是相容的。最近进行了各种理论和光谱研究[3-71]，以确定氧血红素反应性的立体化学起源。低温辐解方法[8，9]在玻璃基质中产生氧-血红素蛋白复合物的单电子加成化合物用于光谱分析的潜在应用在本工作中得到证明。
The oxy-heme unit of oxygen-hemoprotein complexes contains four oxidizing equivalents in excess of the ferrous state. Oneelectronequivalent reduction of the oxy-heme center would therefore convert it formally to the oxidation state of t5. This oxidation state is known to represent the catalytic intermediate compound I of peroxidase enzymes [1, 2]. However, no such intermediate compound has been found in the case of the oxygen storage and transport hemoproteins such as myoglobin and hemoglobin. These results seem to be compatible with the difference in catalytic specificity and reactivity of oxy-heme complexes of heme proteins and enzymes. Various theoretical and spectroscopic studies [3-71 have been recently undertaken to define stereochemical origins of the oxy-heme reactivity. The potential application of low-temperature radiolysis method [8, 9] to produce oneelectron-addition compounds of the oxygen-hemoprotein complexes in glassy matrices for spectroscopic analysis is demonstrated in the present work.