辣根过氧化物酶化合物I低温光解过程中高铁血红素的形成。
The formation of ferric haem during low-temperature photolysis of horseradish peroxidase Compound I.
作者信息
Foote N, Gadsby P M, Berry M J, Greenwood C, Thomson A J
机构信息
School of Biological Sciences, University of East Anglia, Norwich, U.K.
出版信息
Biochem J. 1987 Sep 15;246(3):659-68. doi: 10.1042/bj2460659.
Abstract
Illumination at low temperature of the peroxide compound of horseradish peroxidase (HRP-I) causes partial conversion of the haem electronic structure from a ferryl-porphyrin radical species into a low-spin ferric state. Magnetic-c.d. (m.c.d.) and e.p.r. spectral features of the photolysis product are almost identical with those of the alkaline form of ferric HRP, proposed on the basis of its near-i.r. m.c.d. spectrum to be a Fe(III)-OH species. The ferric product of HRP-I photolysis also contains free-radical e.p.r. signals. Conversion of HRP-I into the Fe(III)-OH species, which requires transfer of a proton and two electrons from the protein, is shown to be a two-step process.
摘要
在低温下照射辣根过氧化物酶的过氧化物化合物（HRP-I）会导致血红素电子结构从铁卟啉自由基物种部分转化为低自旋铁状态。光解产物的磁圆二色性（m.c.d.）和电子顺磁共振（e.p.r.）光谱特征与基于其近红外m.c.d.光谱提出的碱性形式的铁HRP几乎相同，该碱性形式的铁HRP被认为是一种Fe(III)-OH物种。HRP-I光解的铁产物还包含自由基e.p.r.信号。HRP-I转化为Fe(III)-OH物种需要从蛋白质转移一个质子和两个电子，这被证明是一个两步过程。
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