Lytic polysaccharide monooxygenases (LPMOs) catalyze a reaction that is crucial for the biological decomposition of various biopolymers and for the industrial conversion of plant biomass. Despite the importance of LPMOs, the exact molecular-level nature of the reaction mechanism is still debated today. Here, we investigated the pH-dependent conformation of a second-sphere histidine (His) that we call the stacking histidine, which is conserved in fungal AA9 LPMOs and is speculated to assist catalysis in several of the LPMO reaction pathways.

中文翻译：

---

AA9 裂解多糖单加氧酶中第二球组氨酸的旋转异构体具有 pH 依赖性


裂解多糖单加氧酶 (LPMO) 催化的反应对于各种生物聚合物的生物分解和植物生物质的工业转化至关重要。尽管 LPMO 很重要，但反应机制的确切分子水平性质至今仍存在争议。在这里，我们研究了第二球组氨酸 (His) 的 pH 依赖性构象，我们将其称为堆积组氨酸，它在真菌 AA9 LPMO 中保守，推测有助于催化多个 LPMO 反应途径。