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Ligands to the 2Fe iron‐sulfur center in succinate dehydrogenase
Author(s) -
Ævarsson Arnthór,
Hederstedt Lars
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80757-9
Subject(s) - succinate dehydrogenase , cysteine , protein subunit , biochemistry , chemistry , fumarate reductase , stereochemistry , bacillus subtilis , nadh dehydrogenase , peptide sequence , enzyme , biology , gene , bacteria , genetics
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.