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| 猪心肌高铁肌红蛋白高级结构动态信息的光谱指认 | |
| 引用本文： | 李亚东,吴名草,汤 宇,金邦荃,黄鹤勇,李 钢,冯玉英. 猪心肌高铁肌红蛋白高级结构动态信息的光谱指认[J]. 食品科学, 2016, 37(9): 111-116. DOI: 10.7506/spkx1002-6630-201609021 |
| 作者姓名： | 李亚东 吴名草 汤 宇 金邦荃 黄鹤勇 李 钢 冯玉英 |
| 作者单位： | 1.南京师范大学金陵女子学院，江苏 南京 210097；2.南京师范大学分析测试中心，江苏 南京 210097 |
| 摘 要： | 本实验采用扫描电子显微镜、X射线衍射、拉曼、红外等现代光谱技术和数据库、计算软件等，层层剖析猪心肌高铁肌红蛋白（pig metmyoglobin，pMetMb）冻干粉的结构特征和分子动态结构信息。结果表明，pMetMb冻干粉表观呈明显的棱状结晶体，结晶度为（95.60±1.37）%，三晶胞轴长不相等（a≠b≠c），可归属于高晶度含水单斜结晶体。根据晶体数据库同类化合物比对，得到pMetMb肽链和heme-Fe的关键基团来源；经拉曼和红外光谱解析和推算，pMetMb肽链均有α螺旋、β折叠、β转角和无规卷曲4 种蛋白质二级结构，分别占50%、14%、24%和12%；分别由3 个酰胺区中C=O、C=C、C-N、-COO－、C-H、N-H的不同振动形式所产生；六配位低自旋的Fe-C-N形成heme-Fe3+。因此，pMetMb为六配位低自旋构象，是结构紧密、性质稳定的球状蛋白质。 |
| 关 键 词： | 单斜晶体 结构域 动态结构信息 光谱特征 猪心肌高铁肌红蛋白 |
Spectral Assignment of Dynamic Structure Information of Porcine Myocardial Metmyoglobin (pMetMb) |
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| LI Yadong,WU Mingcao,TANG Yu,JIN Bangquan,HUANG Heyong,LI Gang,FENG Yuying. Spectral Assignment of Dynamic Structure Information of Porcine Myocardial Metmyoglobin (pMetMb)[J]. Food Science, 2016, 37(9): 111-116. DOI: 10.7506/spkx1002-6630-201609021 | |
| Authors: | LI Yadong WU Mingcao TANG Yu JIN Bangquan HUANG Heyong LI Gang FENG Yuying |
| Affiliation: | 1. Ginling College, Nanjing Normal University, Nanjing 210097, China;2. Center of Analysis and Testing, Nanjing Normal University, Nanjing 210097, China |
| Abstract: | The dynamic molecular structures and domains of porcine myocardial metmyoglobin (pMetMb) were studied and analyzed by scanning electron microscopy, X-ray diffraction, Raman and Infrared spectroscopy with matched databases and softwares. Obviously prismatic crystalline structures were observed on the surface of lyophilized pMetMb powder. The crystallinity of pMetMb was (95.60 ± 1.37)%, and it was highly crystalline and monoclinic powder because the lengths of its three-dimensional unit cell were inequality (a ≠ b ≠ c). By comparison with crystal databases the source of heme-Fe domain in pMetMb was identified. The Raman and Infrared spectra proved that the peptide chain of pMetMb contained 50% α-helix, 14% β-fold, 24% β-turn and 12% random coil, which came from the different shake forms C=O, C=C, C－N, －COO-, C－H and N－H in the amide I, II and III regions. The heme-Fe domain in pMetMb formed by imidazole group (C3H4N2) binding with Fe3+. So it belonged to globin with compact structure and stable properties. |
| Keywords: | monoclinic crystal structural domain dynamic structural information spectral characteristics porcine myocardial metmyoglobin (pMetMb) |
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