酸铁酶的光谱和DFT计算意味着新的酸铁位结构
Andrew C Weitz1, Nitai Giri2, Jonathan D Caranto2
1Department of Chemistry, Carnegie Mellon University , Pittsburgh, Pennsylvania 15213, United States.
Journal of the American Chemical Society
|August 1, 2017
概括
酸铁蛋白 (FDP) 使用独特的二氧化铁核心结构来排毒氧化 (NO). 在NO和O2循环过程中,将其降低到单μ-不同状态至关重要,而黄单核酸 (FMN) 则起着质子转移的作用.
科学领域:
- 生物化学
- 酵素学
- 生物有机化学
背景情况:
- 铁蛋白 (FDP) 是无氧生物中必不可少的酶,对于排毒氧化 (NO) 和氧气 (O2) 是至关重要的.
- FDPs具有独特的双核铁活性位点,与其他铁结合酶结构相关,但其NO循环能力不同.
- 了解FDP的电子结构和催化机制对于阐明它们在NO和O2代谢中的生物功能至关重要.
研究的目的:
- 使用先进的光谱技术,以电子方式描述FDP的差异性和差异性状态.
- 阐明减少过程中铁芯的结构变化及其对NO和O2循环的影响.
- 研究弗拉单核酸 (FMN) 在FDP的催化机制中的作用.
主要方法:
- 电子磁共振 (EPR) 和Mössbauer光谱仪用于详细的电子表征.
- 用密度函数理论 (DFT) 计算来建模和解释光谱发现和结构假设.
- 与相关二铁蛋白和合成铁复合物的现有数据进行比较.
主要成果:
- 减少时交换合常数 (J) 从+20 cm-1增加到+32 cm-1,表明铁芯的结构变化.
- 光谱和DFT数据表明二桥分离芯在降解到单-分离状态时失去桥.
- 建议的结晶结构的桥梁溶剂分子与光谱数据不一致;建议使用单μ-异性物种作为活性形式.
结论:
- 与NO和O2反应的FDP的催化功能状态是单μ-异性物种,并未准确地通过晶体结构表示.
- 减少导致二铁芯的结构重组,包括桥的损失.
- 弗拉单核酸 (FMN) 在NO循环过程中参与质子转移,突出其在FDP中的双重作用.
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