The lipoate synthase from Escherichia coli is an iron‐sulfur protein

FEBS Letters

Ollagnier-de Choudens, Sandrine¹  Fontecave, Marc¹ 

[1] Laboratoire de Chimie et Biochimie des Centres Rédox Biologiques, DBMS-CB, CEA/CNRS/Université Joseph Fourier, 17 Avenue des Martyrs, 38054 Grenoble, Cedex 09, France

关键词: Lipoate synthase;    Iron-sulfur protein;    C-S bond formation;    Electron paramagnetic resonance;    LS;    lipoate synthase;    BS;    biotin synthase;    ARR;    anaerobic ribonucleotide reductase;    PFL;    pyruvate formate lyase;    EPR;    electron paramagnetic resonance;    DTT;    dithiothreitol;   

DOI  :  10.1016/S0014-5793(99)00694-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown