Characterization of the pH-dependent dissociation of a multimeric metalloproteinStreptomyces rubiginosusxylose isomerase by ESI FT-ICR mass spectrometry
作者： Janne Jänis , Salla Pasanen , Juha Rouvinen , Pirjo Vainiotalo
DOI: 10.1002/JMS.1413
关键词: Ion cyclotron resonance spectrometry 、 Isomerase 、 Streptomyces rubiginosus 、 Chemistry 、 Mass spectrometry 、 Ketose 、 Dissociation (chemistry) 、 Xylose isomerase 、 Chromatography 、 Stereochemistry 、 Electrospray ionization 、 Spectroscopy
摘要: We report an analysis of the pH-dependent dissociation a multimeric metalloprotein, xylose isomerase from Streptomyces rubiginosus (XI), by electrospray ionization (ESI) Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry. Xylose isomerases are industrially significant enzymes that catalyze interconversion aldose and ketose sugars. XI is biologically active as approximately 173-kDa tetrameric complex, comprised four identical 43-kDa subunits eight metal cations, unequivocally identified Mg(2+) cations in this work. ESI FT-ICR spectra measured pH range 3.0-6.9 indicated intact holo-tetramer initiated loss all at
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