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

FEBS Letters

Volumn 453, Issue 1-2, 1999, Pages 25-28

  Choudens, Sandrine Ollagnier De ^a   Fontecave, Marc ^a  

^a UNIV GRENOBLE ALPES   (France)

Author keywords

C S bond formation; Electron paramagnetic resonance; Iron sulfur protein; Lipoate synthase

Indexed keywords

BACTERIAL ENZYME; BIOTIN; IRON SULFUR PROTEIN; OCTANOIC ACID; SULFUR; SYNTHETASE; THIOCTIC ACID;

ANAEROBIC METABOLISM; ARTICLE; CELL INCLUSION; CHEMICAL BINDING; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ESCHERICHIA COLI; GENE CLUSTER; GENE OVEREXPRESSION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ISOLATION; SPECTROSCOPY; ULTRAVIOLET SPECTROSCOPY;

ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; IRON-SULFUR PROTEINS; RECOMBINANT PROTEINS; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFURTRANSFERASES;

EID: 0345120596     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(99)00694-8     Document Type: Article

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