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首页> 外文期刊>European Biophysics Journal >EPR studies of iso-1-cytochrome c: effect of temperature on two-component spectra of spin label attached to cysteine at positions 102 and 47
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EPR studies of iso-1-cytochrome c: effect of temperature on two-component spectra of spin label attached to cysteine at positions 102 and 47

机译：EPR研究异1-细胞色素c：温度对102和47位半胱氨酸上附着的自旋标记的两组分光谱的影响

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摘要

Wild-type iso-1-cytochrome c from Saccharomyces cerevisiae containing naturally occurring cysteine at position 102 and mutated protein S47C (derived from the protein in which C102 had been replaced by threonine) were labeled with cysteine-specific methanethiosulfonate spin label. Continuous wave (CW) electron paramagnetic resonance (EPR) was used to examine the effect of temperature on the behavior of the spin label in the oxidized and reduced forms of wild-type cytochrome c and in the oxidized form of the mutated protein. The computer simulations revealed that the CW EPR spectrum for each form of cytochrome c consists of at least two components [a fast (F) and a slow (S) component], which differ in the values of the rotational correlation times $tau _{{rm R}_parallel } $ (longitudinal rotational correlation time) and $tau _{{rm R}_ bot } $ (transverse rotational correlation time) and that the relative contributions of the F and S components of the spectra change with temperature. In addition, the values of the rotational correlation times ( $tau _{{rm R}_parallel } $ and $tau _{{rm R}_ bot } $ ) for the F component appear to change much more dramatically with the temperature than the respective values for the S component. A large difference between the behavior of the oxidized and reduced wild-type spin-labeled cytochromes c indicates that the temperature-induced unfolding of the protein in the region around C102 progresses more rapidly when cytochrome c is in the oxidized form.
机译：用半胱氨酸特异性甲硫代磺酸盐自旋标记物标记来自酿酒酵母的野生型异-1-细胞色素c，其在位置102处含有天然存在的半胱氨酸和突变的蛋白质S47C（源自已被苏氨酸取代的C102蛋白质）。连续波（CW）电子顺磁共振（EPR）用于检查温​​度对野生型细胞色素c的氧化形式和还原形式以及突变蛋白的氧化形式中自旋标记物行为的影响。计算机模拟表明，每种形式的细胞色素c的CW EPR谱至少包含两个成分[快速（F）和慢速（S）成分]，它们的旋转相关时间乘以$ tau _ { {rm R} _parallel} $（纵向旋转相关时间）和$ tau _ {{rm R} _ bot} $（横向旋转相关时间），并且光谱的F和S分量的相对贡献随温度变化。此外，F分量的旋转相关时间（$ tau _ {{rm r} _parallel} $和$ tau _ {{rm r} _bot} $）的值似乎随温度的变化比变化大得多。 S分量的各个值。氧化型和还原型野生型自旋标记的细胞色素c的行为之间的巨大差异表明，当细胞色素c处于氧化形式时，温度诱导的C102周围区域蛋白质的解折叠进展更快。

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