LIGANDS TO THE FE-2 IRON-SULFUR CENTER IN SUCCINATE-DEHYDROGENASE
LIGANDS TO THE FE-2 IRON-SULFUR CENTER IN SUCCINATE-DEHYDROGENASE
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DOI：
10.1016/0014-5793(88)80757-9
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发表时间：
1988-05-23
期刊：
影响因子：
3.5
通讯作者：
HEDERSTEDT, L
中科院分区：
文献类型：
--
作者：
AEVARSSON, A;HEDERSTEDT, L
膜结合琥珀酸氧化还原酶是含有2Fe、3Fe和4Fe铁硫中心各一个的黄素酶。氨基酸序列同源性表明所有三个中心均位于 Ip (B) 亚基中。通过对枯草芽孢杆菌琥珀酸脱氢酶缺陷突变体的多肽和基因分析结合早期的EPR光谱数据，我们发现Ip前半部分的四个保守的半胱氨酸残基是[2Fe-2S]中心的配体。先前已预测这四个残基是配体。我们的结果还表明 B 的 N 末端部分。 subtilisIp构成一个结构域，该结构域可以单独掺入2Fe中心并与脱氢酶的含黄素亚基Fp相互作用。
Membrane-bound succinate oxidoreductases are flavoenzymes containing one each of a 2Fe, a 3Fe and a 4Fe iron-sulfur center. Amino acid sequence homologies indicate that all three centers are located in the Ip (B) subunit. From polypeptide and gene analysis ofBacillus subtillissuccinate dehydrogenase-defective mutants combined with earlier EPR spectroscopic data, we show that four conserved cysteine residues in the first half of Ip are the ligands to the [2Fe-2S] center. These four residues have previously been predicted to be the ligands. Our results also suggest that the N-terminal part ofB. subtilisIp constitutes a domain which can incorporate separately the 2Fe center and interact with Fp, the flavin-containing subunit of the dehydrogenase.