Fate of the (2Fe-2S)(2+) cluster of Escherichia coli biotin synthase during reaction: a Mössbauer characterization

Biotin synthase, the enzyme which catalyzes the last step of the biosynthesis of biotin, contains only (2Fe-2S)(2+) clusters when isolated under aerobic conditions. Previous results showed that reduction by dithionite or photoreduced deazaflavin converts the (2Fe-2S)(2+) to (4Fe-4S)(2+,+). However,...

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Veröffentlicht in:	Biochemistry (Easton) 2003-07, Vol.42 (29), p.8791-8798
Hauptverfasser:	Tse Sum Bui, Bernadette, Benda, Rüdiger, Schünemann, Volker, Florentin, Dominique, Trautwein, Alfred X, Marquet, Andrée
Format:	Artikel
Sprache:	eng
Schlagworte:	Ammonium Sulfate - pharmacology Dose-Response Relationship, Drug Escherichia coli - enzymology Flavin-Adenine Dinucleotide - pharmacology Iron - metabolism Models, Chemical NADP - metabolism Spectroscopy, Mossbauer - methods Subcellular Fractions Sulfur - metabolism Sulfurtransferases - chemistry
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