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首页> 外文期刊>International Journal of Biological Macromolecules: Structure, Function and Interactions >Boron stabilizes peroxide mediated changes in the structure of heme proteins
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Boron stabilizes peroxide mediated changes in the structure of heme proteins

机译：硼稳定过氧化物介导的血红素蛋白结构变化

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Boron is reported in this study to stabilize the structure of heme proteins exposed to peroxides. The oxidized heme protein (15μM) was treated with H_2O_2 (10mM) in 1M glycine-NaOH buffer (pH 9.2) at 25°C in absence/presence of boron, and characterized by visible absorption spectroscopy, gel exclusion chromatography, native PAGE, HPLC and DLS. Spectral analysis of exposed heme proteins revealed a decrease in absorbance in the Soret region, which was stabilized by boron. The native PAGE analysis of exposed heme proteins showed high molecular weight products; the band intensity was lesser in presence of boron. Further, elution profile of the exposed heme proteins on Sephadex G-200 column and HPLC revealed more than one peak (aggregate formation) when compared to the respective untreated proteins. DLS, which measures the hydrodynamic radius (R_H), was used to ascertain whether the peaks correspond to monomer, dimer or aggregate forms. The R_H of boron pretreated heme proteins was close to R_H of the respective heme protein. Non-heme protein RNase did not show any change when exposed to peroxide. Taken together, results conclude that boron stabilizes the structure of heme proteins, which might be due to specific sites on heme proteins that can bind to borate ions.
机译：这项研究报道了硼来稳定暴露于过氧化物的血红素蛋白的结构。氧化血红素蛋白（15μM）在25°C下，无硼存在下，在1M甘氨酸-NaOH缓冲液（pH 9.2）中用H_2O_2（10mM）处理，并通过可见吸收光谱，凝胶排阻色谱，天然PAGE，HPLC和DLS。暴露的血红素蛋白的光谱分析表明，Soret区的吸光度降低了，这被硼稳定了。暴露的血红素蛋白的天然PAGE分析显示高分子量产物。在硼存在下，带强度较小。此外，与各自未处理的蛋白质相比，Sephadex G-200色谱柱和HPLC上暴露的血红素蛋白质的洗脱曲线显示一个以上的峰（聚集体形成）。使用测量流体力学半径（R_H）的DLS确定峰是否对应于单体，二聚体或聚集体形式。硼预处理的血红素蛋白的R_H接近相应血红素蛋白的R_H。非血红素蛋白RNase暴露于过氧化物时未显示任何变化。两者合计，结果得出结论，硼稳定了血红素蛋白的结构，这可能是由于血红素蛋白上可以结合硼酸根离子的特定位点所致。

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