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首页> 外文会议>American Chemical Society national meeting >Proton NMR Characterization of Recombinant Ferric Heme Domains of the Oxygen Sensors FixL and Dos: Evidence for Protein Heterogeneity
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Proton NMR Characterization of Recombinant Ferric Heme Domains of the Oxygen Sensors FixL and Dos: Evidence for Protein Heterogeneity

机译：氧传感器滤光器和DOS的重组亚血管结构域的质子NMR表征：蛋白质异质性的证据

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Proton NMR studies have been carried out on the oxidized (ferric) forms of recombinant FixL heme domains (FixLH) from two species, Sinorhizobium meliloti (Sm) and Bradyrhizobium japonicum (Bj), and on the recombinant heme domain of the E. coli Dos (EcDosH). Hyperfine resonance spectra of the two FixLHs are quite different, despite their structural similarity. Both display high spin proton spectra with shifts extending over 80 ppm to high frequency. In contrast, the EcDosH spectrum is typically low spin, with hyperfine resonance shifts not extending past 40 ppm to high frequency. Careful examination of these spectra reveal line shape heterogeneity in several hyperfine resonances. The spectra depend on the particular preparation and temperature. Spectra of both FixLHs and DosH display this phenomenon. The heterogeneity is due to protein mass loss, which is detectable by mass spectrometry, but is not due to protease activity.
机译：Proton NMR研究已经在两种物种，Sinorhizobium Meliloti（SM）和Bradyrhizobium（BJ）中的重组夹具血红素结构型（FIXLH）的氧化（FIRRIC）形式的研究中进行，并在大肠杆菌DOS的重组血红素结构域上进行（ecodosh）。尽管它们的结构相似，但两种固定剂的高血速共振光谱是完全不同的。两者都显示高旋转质子谱，换档延伸超过80ppm到高频。相反，eCDOSH光谱通常是低旋转的，高浓度的共振移位未将超过40ppm延伸到高频率。仔细检查这些光谱揭示了几种高浓缩共振中的线形状异质性。光谱取决于特定的制备和温度。两个滤光器和DOSH的光谱显示出这种现象。异质性是由于蛋白质质量损失，其可通过质谱法检测，但不是由于蛋白酶活性。

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