Brudvig G W, Bocian D F, Gamble R C, Chan S I
Biochim Biophys Acta. 1980 Jul 24;624(1):78-89. doi: 10.1016/0005-2795(80)90227-5.
Samples of X-irradiated cytochrome c oxidase were examined by electron paramagnetic resonance and optical spectroscopy. Both radiation from the Stanford Synchrotron Radiation Laboratory and a conventional X-ray source (W target) were utilized. The X-ray flux from these sources ranges from 10(9) to 10(13) photons/s. No evidence was found for photoreduction of the metal centers in the enzyme by X-ray photons. These results demonstrate that the integrity of cytochrome c oxidase is maintained using the conditions under which X-ray absorption measurements are presently being made.
通过电子顺磁共振和光谱学对经X射线辐照的细胞色素c氧化酶样本进行了检测。使用了来自斯坦福同步辐射实验室的辐射以及传统的X射线源(钨靶)。这些源的X射线通量范围为10⁹至10¹³光子/秒。未发现X射线光子使该酶中的金属中心发生光还原的证据。这些结果表明,在目前进行X射线吸收测量的条件下,细胞色素c氧化酶的完整性得以维持。