恶臭假单胞菌苯双加氧酶末端双加氧酶蛋白的穆斯堡尔光谱研究。
Mössbauer spectroscopic studies of the terminal dioxygenase protein of benzene dioxygenase from Pseudomonas putida.
作者信息
Geary P J, Dickson D P
出版信息
Biochem J. 1981 Apr 1;195(1):199-203. doi: 10.1042/bj1950199.
Abstract
Mössbauer spectra obtained from the terminal dioxygenase protein of the benzene dioxygenase system from Pseudomonas putida show that it contains [2Fe--2S] centres similar to those of the two-iron plant-type ferredoxins. In the oxidized form the two iron atoms within the centre are high-spin ferric but with considerable inequivalence. In the reduced form the centre contains one extra electron, and this is localized on one of the iron atoms, which becomes high-spin ferrous.
摘要
从恶臭假单胞菌的苯双加氧酶系统的末端双加氧酶蛋白获得的穆斯堡尔光谱表明，它含有与二铁植物型铁氧化还原蛋白类似的[2Fe-2S]中心。在氧化形式下，中心内的两个铁原子是高自旋铁离子，但具有相当大的不等价性。在还原形式下，该中心含有一个额外的电子，并且该电子定位于其中一个铁原子上，该铁原子变为高自旋亚铁离子。
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