EXXON PRT TIME XRAY ABSORPTION SPECTROSCOPY OF PYROCOCCUS FURIOSUS RUBREDOXIN

X射线吸收光谱已被用来探测冷冻的 红色热还蛋白金属中心的溶液结构 在天然的含铁蛋白质中，锌和 汞取代的蛋白质。对于所有研究的样品，光谱 都被解释为一个协调的壳 硫磺，近似四面体配位。对于本地人来说 蛋白质氧化后的Fe-S键长分别为2.29和2.33E 和还原蛋白质。这些价值观是极好的 与以前从X射线结晶学获得的结果一致。 金属取代的Rubredoxins的金属-硫键长度为 2.34和2.54E，锌和汞取代蛋白， 分别进行了分析。

X-ray absorption spectroscopy has been used to probe the frozen solution structure of the metal site in Pyrococcus furiosus rubredoxin in the native, iron-containing protein, and in zinc and mercury-substituted proteins. For all samples studied, the spectra have been interpreted in terms of a single shell of coordinated sulfur, with approximately tetrahedral coordination. For the native protein we obtain Fe-S bond-lengths of 2.29 and 2.33 E, for oxidized and reduced proteins, respectively. These values are in excellent agreement with those previously obtained from X-ray crystallography. The metal-substituted rubredoxins possess metal-sulfur bond lengths of 2.34 and 2.54 E, for the zinc and mercury-substituted proteins, respectively.