对利用辅酶B12的酶催化过程中观察到的电子顺磁共振光谱的物理解释。
A physical explanation of the EPR spectrum observed during catalysis by enzymes utilizing coenzyme B12.
作者信息
Schepler K L, Dunham W R, Sands R H, Fee J A, Abeles R H
出版信息
Biochim Biophys Acta. 1975 Aug 26;397(2):510-8. doi: 10.1016/0005-2744(75)90141-2.
We have proposed that the "doublet" EPR spectra observed during catalysis by a number of coenzyme B12-requiring enzymes arises from a weak electrostatic exchange interaction between an organic free radical and low spin Co(II), B12r. By varying the magnitude of the exchange of coupling we have quite accurately simulated the published EPR spectra from the enzyme systems: diol dehydrase, glycerol dehydrase, ribonucleotide reductase, and ethanolamine ammon-ia lyase. A dipolar model was shown to be incompatible with the observed properties of these systems.
我们已经提出，许多需要辅酶B12的酶在催化过程中观察到的“双重态”电子顺磁共振（EPR）光谱源于有机自由基与低自旋Co（II）即B12r之间的弱静电交换相互作用。通过改变耦合交换的大小，我们相当准确地模拟了来自以下酶系统的已发表EPR光谱：二醇脱水酶、甘油脱水酶、核糖核苷酸还原酶和乙醇胺氨裂解酶。结果表明，偶极模型与这些系统的观察特性不相符。
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