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High-resolution crystal structures of the solubilized domain of porcine cytochrome b5

机译:高分辨率的晶体结构随着猪细胞色素b5的领域

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摘要

Mammalian microsomal cytochrome b5 has multiple electron-transfer partners that function in various electron-transfer reactions. Four crystal structures of the solubilized haem-binding domain of cytochrome b5 from porcine liver were determined at sub-angstrom resolution (0.76–0.95??) in two crystal forms for both the oxidized and reduced states. The high-resolution structures clearly displayed the electron density of H atoms in some amino-acid residues. Unrestrained refinement of bond lengths revealed that the protonation states of the haem propionate group may be involved in regulation of the haem redox properties. The haem Fe coordination geometry did not show significant differences between the oxidized and reduced structures. However, structural differences between the oxidized and reduced states were observed in the hydrogen-bond network around the axial ligand His68. The hydrogen-bond network could be involved in regulating the redox states of the haem group.
机译:哺乳动物微粒体细胞色素b5有多个功能的电子转换合作伙伴各种各样的电子转换反应。结构的可溶性haem-binding域从猪的肝脏细胞色素b5确定sub-angstrom分辨率(0.76 - -0.95 ? ?)的两种晶体形式氧化和减少。结构清晰显示的电子密度在某些氨基酸残基的H原子。无节制的细化的债券长度显示质子化作用的血红素丙酸组可能参与调节血红素氧化还原性质。协调几何没有显示显著氧化和减少之间的差异结构。在氧化和减少国家之间观察周围形成氢键网络轴向配位体His68。可能参与调节氧化还原状态的血红素组。

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