Sensitive Monitoring of the Dynamics of a Membrane-Bound Transport Protein by Tryptophan Phosphorescence Spectroscopy

This paper presents a tryptophan phosphorescence spectroscopy study on the membrane-bound mannitol transporter, EIImtl, from E. coli. The protein contains four tryptophans at positions 30, 42, 109, and 117. Phosphorescence decays in buffer at 1 °C revealed large variations of the triplet lifetimes o...

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Veröffentlicht in:	Biochemistry (Easton) 2000-09, Vol.39 (35), p.10877-10883
Hauptverfasser:	Broos, Jaap, Strambini, Giovanni B, Gonnelli, Margherita, Vos, Erwin P. P, Koolhof, Michel, Robillard, George T
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding Sites - genetics Biological Transport - genetics Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cysteine - chemistry Cysteine - metabolism Escherichia coli - enzymology Escherichia coli - genetics Escherichia coli Proteins Freezing Glass Histidine - chemistry Histidine - metabolism Luminescent Measurements Mannitol - chemistry Mannitol - metabolism Membrane Proteins - chemistry Membrane Proteins - genetics Membrane Proteins - metabolism Monosaccharide Transport Proteins Mutagenesis, Site-Directed Phosphoenolpyruvate Sugar Phosphotransferase System - chemistry Phosphoenolpyruvate Sugar Phosphotransferase System - genetics Phosphoenolpyruvate Sugar Phosphotransferase System - metabolism Phosphorylation Solutions Spectrometry, Fluorescence - methods Thermodynamics Tryptophan - chemistry Tryptophan - genetics
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Zusammenfassung:	This paper presents a tryptophan phosphorescence spectroscopy study on the membrane-bound mannitol transporter, EIImtl, from E. coli. The protein contains four tryptophans at positions 30, 42, 109, and 117. Phosphorescence decays in buffer at 1 °C revealed large variations of the triplet lifetimes of the wild-type protein and four single-tryptophan-containing mutants. They ranged from
ISSN:	0006-2960 1520-4995
DOI:	10.1021/bi000803z