Die Rolle des Thiolatliganden in Hämproteinen

硫醇配体在血红素蛋白中的作用

• 批准号: 5176966
• 负责人: Professor Dr. Volker Ullrich
• 金额: --
• 依托单位: Fachbereich Biologie
• 依托单位国家: 德国
• 项目类别: Priority Programmes
• 财政年份: 1999
• 资助国家: 德国
• 起止时间: 1998-12-31 至 2003-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/5176966?language=en
• 关键词: Die; Rolle; des; Thiolatliganden; mproteinen

Heme-thiolate proteins or cytochrome P450 enzymes are of mechanistical interest because of their special catalytic abilities in performing hydroxylations, epoxidations, halogenations or rearrangements of peroxides. Based on our previous work and the resulting working hypothesis the electronic interaction of the negatively charged sulfur with heme in its higher oxidation states leads to stabilized but still reactive thiyl intermediates, from which the ferryl and perferryl ion linked to the redox-active sulfur play a special role in the catalysis of radical reactions. We succeeded for the first time to spectroscopically identify a ferryl complex of a heme-thiolate protein (P450NOR). Such investigations will be expanded to P450BM-3 and the reactivities of the ferryl and perferryl intermediates will be compared to those of the non-thiolate heme proteins.

血红素硫醇蛋白或细胞色素 P450 酶因其在过氧化物的羟基化、环氧化、卤化或重排方面具有特殊的催化能力而受到机械学的关注。根据我们之前的工作和由此产生的工作假设，带负电的硫与处于较高氧化态的血红素的电子相互作用产生稳定但仍具有反应性的硫基中间体，其中与氧化还原活性硫连接的铁基和过铁基离子在自由基反应的催化中发挥特殊作用。我们首次成功地通过光谱鉴定了血红素硫醇蛋白（P45​​0NOR）的ferryl复合物。此类研究将扩展到 P450BM-3，并将ferry1 和perferryl 中间体的反应性与非硫醇盐血红素蛋白的反应性进行比较。