BIOLOGICAL METAL CLUSTERS BIOPHYSICAL & MODEL STUDIES

生物金属簇 生物物理

• 批准号: 6120379
• 负责人: MICHAEL J MARONEY
• 金额: --
• 依托单位: ALBERT EINSTEIN COLLEGE OF MEDICINE
• 依托单位国家: 美国
• 财政年份: 1998
• 资助国家: 美国
• 起止时间: 1998-09-30 至 1999-08-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6120379
• 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.

我们还完成了第一个特征的积极 首尔链霉菌NiSOD的酶切位点。 这项研究表明， Ni位点与硫醇盐供体结合，像其他Ni氧化还原酶一样，但 不同于任何先前表征的SOD。 检查氧化和 减少的样品揭示了配位数的变化（5 -> 4）和 边缘能量的移动适合于单电子过程。 也有证据表明，活性部位由两个Ni 中心，其中之一与CuZnSOD类似不是氧化还原活性的， 因此必须由四聚体中的两个亚基组成 酵素