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The lipoate synthase from Escherichia coli is an iron‐sulfur protein
Author(s) -
Ollagnier-de Choudens Sandrine,
Fontecave Marc
Publication year - 1999
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/s0014-5793(99)00694-8
Subject(s) - escherichia coli , sulfur , chemistry , biochemistry , atp synthase , microbiology and biotechnology , biology , enzyme , organic chemistry , gene
Lipoate synthase catalyzes the last step of the biosynthesis of lipoic acid in microorganisms and plants. The protein isolated from an overexpressing Escherichia coli strain was purified from inclusion bodies. Spectroscopic (UV‐visible and electron paramagnetic resonance) properties of the reconstituted protein demonstrate the presence of a (2Fe‐2S) center per protein. As observed in biotin synthase, these clusters are converted to (4Fe‐4S) centers during reduction under anaerobic conditions. The possible involvement of the cluster in the insertion of sulfur atoms into the octanoic acid backbone is discussed.