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首页> 外文期刊>Biochemistry >Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties
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Atomic resolution crystal structures, EXAFS, and quantum chemical studies of rusticyanin and its two mutants provide insight into its unusual properties

机译：Rustyanyanin及其两个突变体的原子分辨率晶体结构，EXAFS和量子化学研究提供了对其不寻常特性的洞察力

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Rusticyanin from the extremophile Thiobacillus ferrooxidans is a blue copper protein with unusually high redox potential and acid stability. We present the crystal structures of native rusticyanin and of its Cu site mutant His143Met at 1.27 and 1.10 angstrom, respectively. The very high resolution of these structures allows a direct comparison with EXAFS data and with quantum chemical models of the oxidized and reduced forms of the proteins, based upon both isolated and embedded clusters and density functional theory (DFT) methods. We further predict the structure of the Cu(II) form of the His143Met mutant which has been experimentally inaccessible due to its very high redox potential. We also present metrical EXAFS data and quantum chemical calculations for the oxidized and reduced states of the Met148Gln mutant, this protein having the lowest redox potential of all currently characterized mutants of rusticyanin. These data offer new insights into the structural factors which affect the redox potential in this important class of proteins. Calculations successfully predict the structure and the order of redox potentials for the three proteins. The calculated redox potential of H143M (similar to 400 mV greater than native rusticyanin) is consistent with the failure of readily available chemical oxidants to restore a Cu(II) species of this mutant. The structural and energetic effects of mutating the equatorial cysteine to serine, yet to be studied experimentally, are predicted to be considerable by our calculations.
机译：来自极端嗜热铁氧体硫氧化硫杆菌的质朴花青素是一种蓝色铜蛋白，具有极高的氧化还原电位和酸稳定性。我们目前在1.27和1.10埃呈现天然rustyanyanin及其铜位突变His143Met的晶体结构。这些结构的非常高的分辨率可以与EXAFS数据以及基于氧化和还原形式的蛋白质的量子化学模型进行直接比较，该模型基于分离的和嵌入的簇以及密度泛函理论（DFT）方法。我们进一步预测了His143Met突变体的Cu（II）形式的结构，由于其非常高的氧化还原潜力，该突变体在实验上无法获得。我们还提供了Met148Gln突变体的氧化态和还原态的度量EXAFS数据和量子化学计算，该蛋白质在所有目前表征的Rustyanyanin突变体中具有最低的氧化还原电位。这些数据提供了对影响这一重要蛋白质类别中氧化还原电位的结构因素的新见解。计算成功地预测了这三种蛋白质的结构和氧化还原电位的顺序。 H143M的计算出的氧化还原电位（大约比天然的rusticalyanin高400 mV）与现成的化学氧化剂无法还原该突变体的Cu（II）物种相一致。由我们的计算预测，尚需进行实验研究的将赤道半胱氨酸突变为丝氨酸的结构和能量效应相当可观。

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