The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity.
作者： Pattraranee Limphong , Ross M. McKinney , Nicole E. Adams , Christopher A. Makaroff , Brian Bennett
DOI: 10.1007/S00775-009-0593-6
关键词: Catalysis 、 Enzyme kinetics 、 Electron paramagnetic resonance 、 Inorganic chemistry 、 Metal 、 Zinc 、 Substrate (chemistry) 、 Selectivity 、 Kinetics 、 Chemistry
摘要: In an effort to better understand the structure, metal content, nature of centers, and enzyme activity Arabidopsis thaliana Glx2-2, was overexpressed, purified, characterized using analyses, kinetics, UV–vis, EPR, 1H NMR spectroscopies. Glx2-2-containing fractions that were purple, yellow, or colorless separated during purification, differently colored found contain different amounts Fe Zn(II). Spectroscopic analyses discrete provided evidence for Fe(II), Fe(III), Fe(III)–Zn(II), antiferromagnetically coupled Fe(II)–Fe(III) centers distributed among fractions. The individual steady-state kinetic constants varied fractionated species, depending on number type ion present. Intriguingly, however, catalytic efficiency constant, kcat/Km, invariant value kcat/Km governs rate at low, physiological substrate concentrations. We suggest independence precise makeup active-site center is evolutionarily related lack selectivity either versus Zn(II) Fe(II) in one more binding sites.
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