EXAFS reveals a structural zinc binding site in the bovine NADH-Q oxidoreductase

The metal content of bovine NADH-Q oxidoreductase determined by inductively-coupled plasma atomic-emission spectroscopy reveals the presence of about one atom of zinc per molecule of flavin mononucleotide. We applied Zn K-edge extended X-ray absorption fine structure spectroscopy (EXAFS) to investig...

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Veröffentlicht in:	FEBS letters 2007-12, Vol.581 (29), p.5645-5648
Hauptverfasser:	Giachini, Lisa, Francia, Francesco, Boscherini, Federico, Pacelli, Consiglia, Cocco, Tiziana, Papa, Sergio, Venturoli, Giovanni
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Binding Sites Cattle Cysteine - chemistry Cysteine - metabolism EXAFS extended X-ray absorption fine structure spectroscopy Histidine - chemistry Histidine - metabolism ICP-AES inductively-coupled plasma atomic-emission spectroscopy Models, Molecular NADH-Q oxidoreductase polyvinyl alcohol PVA Quinone Reductases - chemistry Quinone Reductases - metabolism Spectrophotometry Spectrum Analysis Structure-Activity Relationship X-ray diffraction X-Rays XRD Zinc - chemistry Zinc - metabolism Zinc binding site
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