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首页> 外文期刊>Biochemistry >Structure and Dynamics of Reduced Bacillus pasteurii Cytochrome c: Oxidation State Dependent Properties and Implications for Electron Transfer Processes.
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Structure and Dynamics of Reduced Bacillus pasteurii Cytochrome c: Oxidation State Dependent Properties and Implications for Electron Transfer Processes.

机译:减少的巴斯德芽孢杆菌细胞色素c的结构和动力学:取决于氧化态的性质及其对电子转移过程的影响。

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摘要

The solution structure of reduced Bacillus pasteurii cytochrome c, which has only 71 amino acids, has been determined by NMR to an RMSD of 0.46 +/- 0.08 A for all backbone atoms and 0.79 +/- 0.08 A for all heavy atoms and refined through restrained energy minimization. The target function out of 1645 constraints is 0.52 +/- 0.11 A(2), and the penalty function is 66 +/- 12 kJ mol(-)(1). The structure appears very similar to that in the oxidized state, only Trp87 and the propionates showing significant differences. The mobility was investigated through (15)N R(1) and R(2) relaxation rates, (15)N-(1)H NOE, and (1)H/(2)H exchange. It is found that the oxidized form is generally more mobile than the reduced one. By comparing the redox-state dependence of the structural/dynamic properties of Fe-S proteins, cytochrome c, and blue copper proteins, hints are provided for a better comprehension of the electron transfer processes.
机译:经核磁共振测定,所有骨架原子的RMSD为0.46 +/- 0.08 A,所有重原子为0.79 +/- 0.08 A,经还原的巴斯德毕赤酵母细胞色素c的溶液结构仅具有71个氨基酸,并通过限制能量最小化。 1645个约束中的目标函数为0.52 +/- 0.11 A(2),惩罚函数为66 +/- 12 kJ mol(-)(1)。该结构看起来与氧化态非常相似,只有Trp87和丙酸酯显示出显着差异。通过(15)N R(1)和R(2)弛豫率,(15)N-(1)H NOE和(1)H /(2)H交换研究了迁移率。发现氧化态通常比还原态更易移动。通过比较Fe-S蛋白,细胞色素c和蓝铜蛋白的结构/动力学性质的氧化还原状态依赖性,为更好地理解电子转移过程提供了提示。

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