Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra.
Desulfovibrio vulgaris hydrogenase: a nonheme iron enzyme lacking nickel that exhibits anomalous EPR and Mössbauer spectra.
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普通脱硫弧菌氢化酶：一种缺乏镍的非血红素铁酶，表现出异常的 EPR 和穆斯堡尔谱。
DOI：
10.1073/pnas.81.12.3728
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发表时间：
1984
影响因子：
11.1
通讯作者：
LeGall,J
中科院分区：
文献类型：
--
作者：
Huynh,BH;Czechowski,MH;Krüger,HJ;DerVartanian,DV;PeckJr,HD;LeGall,J
报道了从脱硫弧菌（Desulfovibrio vulgaris）（Hildenborough，National Collection of Industrial Bacteria 8303）中纯化周质氢化酶的方法。纯化的氢化酶具有每毫克蛋白质4800单位的比活性。等离子体发射研究表明，这种高活性氢化酶不含镍，每个分子含有11（+/- 1）个非血红素铁原子。结合EPR和穆斯堡尔研究表明，大多数铁原子以铁-硫簇的形式结合。两个铁氧还蛋白类型的[4Fe-4S]团簇已经被确定，表现出正常的EPR和穆斯堡尔参数;然而，没有3Fe团簇的痕迹被穆斯堡尔测量检测到。在氧化剂，细胞色素c3，和CO的存在下，观察到异常EPR和穆斯堡尔谱指示非典型的非血红素铁中心。
A purification procedure for the periplasmic hydrogenase from Desulfovibrio vulgaris ( Hildenborough , National Collection of Industrial Bacteria 8303) is reported. The purified hydrogenase has a specific activity of 4800 units per mg of protein. Plasma emission studies reveal that this highly active hydrogenase is free of nickel and contains 11 (+/- 1) nonheme iron atoms per molecule. A combined EPR and Mössbauer study indicates that the majority of the iron atoms are bound in the form of iron- sulfur clusters. Two ferredoxin-type [4Fe-4S] clusters have been identified that exhibit normal EPR and Mössbauer parameters; however, no trace of 3Fe cluster is detected by the Mössbauer measurement. In the presence of oxidants, cytochrome c3, and CO, anomalous EPR and Mössbauer spectra indicative of atypical nonheme iron centers are observed.