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 红色激烈热球菌中金属中心的溶液结构 在天然的含铁蛋白质中，在锌和 汞替代蛋白质 对于研究的所有样品，光谱 都被解释为一个单一的协调外壳， 硫，具有近似四面体配位。 针对所述本地 蛋白质，我们得到的Fe-S键长为2.29和2.33 E，为氧化 和减少的蛋白质。 这些价值观在优秀 与以前从X射线晶体学获得的结果一致。 所述金属取代的红曲霉毒素具有的金属-硫键长度为 2.34和2.54 E，对于锌和汞取代的蛋白质， 分别

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.