Ligands to the 2Fe iron‐sulfur center in succinate dehydrogenase

FEBS Letters

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