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首页> 外文期刊>Journal of biological inorganic chemistry: JBIC: a publication of the Society of Biological Inorganic Chemistry >Erratum to: Assignment of the~ 1H NMR resonances of protein residues in close proximity to the heme of the nitrophorins: similarities and differences among the four proteins from the saliva of the adult blood-sucking insect Rhodnius prolixus
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Erratum to: Assignment of the~ 1H NMR resonances of protein residues in close proximity to the heme of the nitrophorins: similarities and differences among the four proteins from the saliva of the adult blood-sucking insect Rhodnius prolixus

机译：勘误如下：接近于氮荧光素血红素的蛋白质残基的〜1H NMR共振分配：成年吸血昆虫Rhodnius prolixus唾液中的四种蛋白质之间的异同

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Correction to the caption of Fig. 3, Table 1, and the text. Further research [Abriata LA, Zaballa M-E, Berry RE, Yang F, Zhang H, Walker FA, Vila AJ, submitted to Inorg Chem] has shown that the small peak seen at 2.6 ppm of the F1 dimension of the WEFT-NOESY spectrum of NP2(D1A) (top right in Fig. 3) decreases in intensity slowly as a function of the amount of time the protein sample has been in D_2O. The spectrum shown in Fig. 3 top right was recorded approximately 1 week after the protein had been dissolved in D_2O containing phosphate buffer at pH* 7.0. The intensity of the peak at 2.6 ppm is about 10 % that of the peak at -2 ppm. However, a similar sample left in D_2O for 16 months showed this peak at 2.6 ppm to have only ~1 % of the intensity of the peak at -2 ppm. Thus this cross peak is that of an exchangeable proton, and cannot be that of the α-CH of His57. By analogy, those of wt NP2 and wt NP3 also shown in the top portion of that figure, and also the 1D NOE shown in the bottom portion of that figure, at similar chemical shifts of 2–3 ppm in each case, are likely exchangeable protons and thus cannot be assigned to the α-CH proton of His57 in these high-spin ferriheme proteins. In the work quoted above by Abriata et al., the α-CH proton of His57 of native N terminus NP2 containing~ (13)C,~ (15)N labeled histidine was shown by~ 1H{~(13)C} HMQC to be at -1.4 ppm. Since native N terminus NP2 and NP2(D1A) have all other proton chemical shifts the same within ~0.2 ppm [Berry RE, Muthu D, Shokhireva TK, Garrett SA, Zhang H, Walker FA (2012) Chem Biodiv 9:1739], we should expect to see a cross peak at -1.4 ± 0.2 ppm for the α-CH of His57 in Fig. 3; however, because of the proximity of the cross peak for the β-CH at about -2 ppm, which is expected to be more intense, that α-CH cross peak is not observed by WEFT-NOESY methods. In the paper by Abriata et al. referenced above, Supporting Information Figure S4 presents the raw data which confirm that the WEFT-NOESY cross peak in the spectrum of NP2(D1A) at 2–3 ppm is that of an exchangeable proton. The same work of Abriata et al., quoted above, shows that the cross peak at 2.90 ppm in the~ 1H–~(13)C plane of the HNCA spectrum of high-spin native N terminus NP2 is that of the backbone amide proton of His57, which is only 2.51 ? from the closest β-CH proton, well within the distance expected for observing NOE cross peaks; in contrast, the α-CH proton is 2.86 ? from that same β-CH proton (PDB file 2EU7, of NP2(D1A)-NH3).
机译：更正了图3，表1和文本的标题。进一步的研究[提交给Inorg Chem的Abriata LA，Zaballa ME，Berry RE，Yang F，Zhang H，Walker FA，Vila AJ提交]，该小峰出现在WEFT-NOESY光谱F1尺寸的2.6 ppm处。 NP2（D1A）（图3右上角）的强度随着蛋白质样品进入D_2O的时间而缓慢降低。蛋白质溶解在pH * 7.0的含D_2O磷酸盐缓冲液中大约1周后，记录了图3右上方的光谱。 2.6 ppm处的峰强度约为-2 ppm处的峰强度的10％。但是，在D_2O中放置16个月的类似样品显示，该峰在2.6 ppm时只有-2 ppm峰强度的〜1％。因此，该交叉峰是可交换质子的峰，而不能是His57的α-CH的峰。以此类推，wt NP2和wt NP3的那些也显示在该图的顶部，以及该图的底部显示的一维NOE，在每种情况下，其化学位移均为2-3 ppm，它们很可能可以互换。质子，因此不能分配给这些高旋铁蛋白血红素蛋白中His57的α-CH质子。在上述Abriata等人的著作中，含有〜（13）C，〜（15）N标记的组氨酸的天然N末端NP2的His57的His57的α-CH质子由〜1H {〜（13）C} HMQC表示。为-1.4 ppm。由于天然N末端NP2和NP2（D1A）的所有其他质子化学位移均在约0.2 ppm之内[Berry RE，Muthu D，Shokhireva TK，Garrett SA，Zhang H，Walker FA（2012）Chem Biodiv 9：1739]，我们应该期望在图3中看到His57的α-CH的交叉峰在-1.4±0.2 ppm处;但是，由于β-CH的交叉峰接近于-2 ppm（预计会更强），因此通过WEFT-NOESY方法未观察到α-CH交叉峰。在Abriata等人的论文中。上面引用的支持信息，图S4提供了原始数据，这些数据证实NP2（D1A）光谱中2-3 ppm处的WEFT-NOESY交叉峰是可交换质子的峰。上面引用的Abriata等人的相同工作表明，高旋转天然N末端NP2的HNCA光谱的〜1H–〜（13）C平面中2.90 ppm处的交叉峰是骨架酰胺质子的交叉峰His57的2.51？从最接近的β-CH质子开始，在预期观察NOE交叉峰的距离之内;相反，α-CH质子为2.86Ω。来自相同的β-CH质子（PDB文件2EU7，NP2（D1A）-NH3）。

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