FEBS Letters | |
Ligands to the 2Fe iron‐sulfur center in succinate dehydrogenase | |
Hederstedt, Lars1  Ævarsson, Arnthór1  | |
[1] Department of Microbiology, University of Lund, Sölvegatan 21, S-223 62 Lund, Sweden | |
关键词: Structural mutant; Iron-sulfur protein; sdh gene; Succinate oxidoreductase; Nonsense mutation; (B. subtilis); | |
DOI : 10.1016/0014-5793(88)80757-9 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
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 of Bacillus subtillis succinate 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 of B. subtilis Ip constitutes a domain which can incorporate separately the 2Fe center and interact with Fp, the flavin-containing subunit of the dehydrogenase.
【 授权许可】
Unknown
【 预 览 】
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