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Spectral Assignment of Dynamic Structure Information of Porcine Myocardial Metmyoglobin (pMetMb)

LI Yadong1, WU Mingcao1, TANG Yu1, JIN Bangquan1,*, HUANG Heyong2, LI Gang2, FENG Yuying2   

  1. 1. Ginling College, Nanjing Normal University, Nanjing 210097, China;
    2. Center of Analysis and Testing, Nanjing Normal University, Nanjing 210097, China
  • Online:2016-05-15 Published:2016-05-18

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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.

Key words: monoclinic crystal, structural domain, dynamic structural information, spectral characteristics, porcine myocardial metmyoglobin (pMetMb)

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