The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mössbauer characterization.
The iron-sulfur centers of the soluble [NiFeSe] hydrogenase, from Desulfovibrio baculatus (DSM 1743). EPR and Mössbauer characterization.
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来自杆状脱硫弧菌 (DSM 1743) 的可溶性 [NiFeSe] 氢化酶的铁硫中心。
DOI：
10.1111/j.1432-1033.1990.tb15499.x
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
Huynh,BH
中科院分区：
文献类型：
--
作者：
Teixeira,M;Moura,I;Fauque,G;Dervartanian,DV;Legall,J;PeckJr,HD;Moura,JJ;Huynh,BH
来自 Desulfovibrio baculatus (DSM 1743) 的可溶性（细胞质加周质）含 Ni/Fe-S/Se 的氢化酶是从富含 57Fe 的培养基中生长的细胞中纯化出来的，其铁硫中心通过穆斯堡尔谱和 EPR 光谱进行了广泛的表征。数据分析排除了 [3Fe-4S] 中心的存在，无论是在天然状态（分离状态）还是在氢还原状态。在天然状态下，非血红素铁原子排列为两个抗磁性 [4Fe-4S]2+ 中心。还原后，这两个中心表现出独特且不寻常的穆斯堡尔光谱参数。通过氧化还原滴定和 EPR 测定，发现这些中心具有相似的中点电位（∼315 mV）。
The soluble (cytoplasmic plus periplasmic) Ni/Fe‐S/Se‐containing hydrogenase fromDesulfovibrio baculatus(DSM 1743) was purified from cells grown in an57Fe‐enriched medium, and its iron‐sulfur centers were extensively characterized by Mössbauer and EPR spectroscopies. The data analysis excludes the presence of a [3Fe‐4S] center, either in the native (as isolated) or in the hydrogen‐reduced states. In the native state, the non‐heme iron atoms are arranged as two diamagnetic [4Fe‐4S]2+centers. Upon reduction, these two centers exhibit distinct and unusual Mössbauer spectroscopic parameters. The centers were found to have similar mid‐point potentials (∼– 315 mV) as determined by oxidation‐reduction titrations followed by EPR.