Nitrosative stress and NO detoxifying reaction mechanisms in microbial nonheme diiron proteins

项目摘要 金属酶在整个人类健康中起着至关重要的作用，并控制着分子氧（O2）的生物化学， 一氧化氮（NO）。病原生物体依赖于血红素和非血红素含铁蛋白质来对抗 人体免疫反应和生存暴露于高浓度的活性氧和氮 种（ROS/RNS）。莫恩-洛科兹实验室结合了经典的生化技术、共振拉曼 (RR)FTIR和EPR光谱与时间分辨技术探测微生物酶系统 其特征在于X射线晶体学，但催化策略仍然知之甚少或完全 未知在这个项目中，最近的一个新的分枝杆菌二铁蛋白的晶体结构， 巨噬细胞感染在显示出独特的结构特征和对 RNS在生物学或无机化学中从未见过。

PROJECT SUMMARY Metalloenzymes play crucial roles throughout human health and govern the biochemistry of dioxygen (O2) and nitric oxide (NO). Pathogenic organisms depend on heme and nonheme iron-containing proteins to counter the human immune response and to survive exposure to high concentrations of reactive oxygen and nitrogen species (ROS/RNS). The Moënne-Loccoz Lab combines classic biochemical techniques, resonance Raman (RR), FTIR, and EPR spectroscopies with time-resolved techniques to probe microbial enzymatic systems characterized by X-ray crystallography, but with catalytic strategies that remain poorly understood or totally unknown. In this project, a recent crystal structure of a novel mycobacterial diiron protein upregulated upon macrophage infection is targeted for investigation after showing unique structural features and reactivity toward RNS never seen before in biology or inorganic chemistry.