AUTOFIT 1 2, UPDATED SOFTWARE FOR XAS GLOBAL MAPPING

AUTOFIT 1 2，XAS 全球地图更新软件

• 批准号: 6205756
• 负责人: MARK R CHANCE
• 金额: $ 2.8万
• 依托单位: ALBERT EINSTEIN COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 1999
• 资助国家: 美国
• 起止时间: 1999-09-01 至 2000-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6205756
• 关键词: bacteria; biological products; biomedical resource; enzymes; proteins; spectrometry

We have also completed the first characterization of the active site of NiSOD from Streptomyces seoulensis. This study reveals that Ni site is bound to thiolate donors, like other Ni redox enzymes but unlike any previously characterized SOD. Examination of oxidized and reduced samples reveal a coordination number change (5 -> 4) and a shift in the edge energy appropriate for a one-electron process. There is also evidence that the active site consists of two Ni centers, one of which is not redox active in analogy with the CuZnSOD, and therefore must be composed of two subunits in the tetrameric enzyme.

我们还完成了对活跃分子的第一次刻画 发酵链霉菌NiSOD的结合部位。这项研究表明， 镍位点与硫酸盐供体结合，就像其他镍氧化还原酶一样，但 不同于任何先前表征的超氧化物歧化酶。氧化态和氧化态的检验 还原的样本显示配位数改变(5->4)和 适用于单电子过程的边缘能量的移动。 还有证据表明，活性中心由两个镍组成 中心，其中一个不是氧化还原活性的，类似于CuZnSOD， 因此必须由四聚体中的两个亚基组成 酵素。