Ferredoxin has a pivotal role in the biosynthesis of the hydrogen-oxidizing hydrogenases in Escherichia coli
Ferredoxin has a pivotal role in the biosynthesis of the hydrogen-oxidizing hydrogenases in Escherichia coli
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DOI：
10.1016/j.ijhydene.2014.03.124
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发表时间：
2014-10-31
影响因子：
7.2
通讯作者：
Sawers, R. Gary
中科院分区：
文献类型：
--
作者：
Jaroschinsky, Monique;Sawers, R. Gary
铁硫簇（FeS）是[NiFe]-氢化酶（Hyd）电子转移小亚基中必不可少的辅因子。在这项研究中，我们分析了铁氧还蛋白在大肠杆菌中三种Hyd生物合成中的体内作用。我们的研究结果表明，fdx突变体，这是无法合成铁氧还蛋白，缺乏氢氧化酶Hyd-1和Hyd-2的活性。在Hyd-2的情况下，这是由于缺乏含FeS簇的小亚基。在Hyd-1的情况下，催化亚基的稳定性也受损。释放氢的Hyd-3酶的部分活性，以及两种呼吸性甲酸脱氢酶的部分活性保留在fdx突变体中。lacZ融合的分析表明，fdx突变对编码Hyd-1的操纵子的表达具有有限的影响。相反，这些数据表明，铁氧还蛋白在成熟或组装的氢氧化[NiFe]-氢化酶的作用。版权所有（C）2014，氢能出版物有限责任公司。由爱思唯尔有限公司发布。保留所有权利。
Iron sulphur clusters (FeS) are essential cofactors in the small, electron-transfer subunits of [NiFe]-hydrogenases (Hyd). In this study we analyzed the in vivo role of ferredoxin in the biosynthesis of three of the Hyd in Escherichia coli. Our results reveal that a fdx mutant, which is unable to synthesize ferredoxin, lacks the activity of both hydrogen-oxidizing enzymes Hyd-1 and Hyd-2. In the case of Hyd-2 this was due to the absence of the FeS cluster-containing small subunit. In the case of Hyd-1, stability of the catalytic subunit was also impaired. Partial activity of the hydrogen-evolving Hyd-3 enzyme, as well as that of both respiratory formate dehydrogenases was retained in the fdx mutant. Analysis of lacZ fusions demonstrated that the fdx mutation had a limited effect on expression of the operon encoding Hyd-1. Rather, these data suggest that ferredoxin has a role in the maturation or assembly of the hydrogen-oxidizing [NiFe]-hydrogenases. Copyright (C) 2014, Hydrogen Energy Publications, LLC. Published by Elsevier Ltd. All rights reserved.