研究揭示葉綠素生物合成酶促光催化的結構基礎
作者:
小柯機器人發布時間:2019/10/25 10:53:54
葉綠素生物合成中酶促光催化的結構基礎,這一成果由英國曼徹斯特大學Nigel S. Scrutton、中國農業科學院程奇和上海交通大學周愛武等研究人員合作取得。2019年10月23日,《自然》雜誌在線發表了這項成果。
研究人員報導了從Thermosynechococcus elongatus和Synechocystis sp的原葉綠素酸酯氧化還原酶(POR)晶體結構,包括游離形式和與煙醯胺輔酶複合的形成。研究人員的原葉綠素酸酯–NADPH–POR三元複合物結構模型和模擬確定了POR活性位點中的多種相互作用,這對於原葉綠素酸酯的結合、光敏化和光化學轉化為葉綠素很重要。
研究人員證明了使用POR變體和原葉綠素類似物進行實驗時,活性位點結構和原葉綠素結構在驅動POR光化學中的重要性。這些研究揭示了,POR活性位點如何通過從NADPH進行的局部氫化物轉移和沿結構定義的質子轉移途徑的遠距離質子轉移,來促進光碟機動的原葉綠素酸酯減少。
據了解,POR催化葉綠素生物合成中的光依賴性步驟,這對光合作用至關重要,並且最終對地球上的所有生命至關重要。POR是三種已知的光依賴性酶之一,它催化光敏劑和底物原葉綠素的還原,形成色素葉綠素。儘管其生物學重要性,POR光催化的結構基礎仍然未知。
附:英文原文
Title: Structural basis for enzymatic photocatalysis in chlorophyll biosynthesis
Author: Shaowei Zhang, Derren J. Heyes, Lingling Feng, Wenli Sun, Linus O. Johannissen, Huanting Liu, Colin W. Levy, Xuemei Li, Ji Yang, Xiaolan Yu, Min Lin, Samantha J. O. Hardman, Robin Hoeven, Michiyo Sakuma, Sam Hay, David Leys, Zihe Rao, Aiwu Zhou, Qi Cheng, Nigel S. Scrutton
Issue&Volume: 2019-10-23
Abstract: The enzyme protochlorophyllide oxidoreductase (POR) catalyses a light-dependent step in chlorophyll biosynthesis that is essential to photosynthesis and, ultimately, all life on Earth1,2,3. POR, which is one of three known light-dependent enzymes4,5, catalyses reduction of the photosensitizer and substrate protochlorophyllide to form the pigment chlorophyllide. Despite its biological importance, the structural basis for POR photocatalysis has remained unknown. Here we report crystal structures of cyanobacterial PORs from Thermosynechococcus elongatus and Synechocystis sp. in their free forms, and in complex with the nicotinamide coenzyme. Our structural models and simulations of the ternary protochlorophyllide–NADPH–POR complex identify multiple interactions in the POR active site that are important for protochlorophyllide binding, photosensitization and photochemical conversion to chlorophyllide. We demonstrate the importance of active-site architecture and protochlorophyllide structure in driving POR photochemistry in experiments using POR variants and protochlorophyllide analogues. These studies reveal how the POR active site facilitates light-driven reduction of protochlorophyllide by localized hydride transfer from NADPH and long-range proton transfer along structurally defined proton-transfer pathways.
DOI: 10.1038/s41586-019-1685-2
Source: https://www.nature.com/articles/s41586-019-1685-2