Structural basis for enzymatic photocatalysis in chlorophyll biosynthesis

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 () and Nigel S. Scrutton ()
Additional contact information
Shaowei Zhang: The University of Manchester
Derren J. Heyes: The University of Manchester
Lingling Feng: Shanghai Jiao Tong University School of Medicine
Wenli Sun: Chinese Academy of Agricultural Sciences
Linus O. Johannissen: The University of Manchester
Huanting Liu: C4-101, Nitrogen Fixation Laboratory, Qi Institute
Colin W. Levy: The University of Manchester
Xuemei Li: Institute of Biophysics, Chinese Academy of Sciences
Ji Yang: C4-101, Nitrogen Fixation Laboratory, Qi Institute
Xiaolan Yu: C4-101, Nitrogen Fixation Laboratory, Qi Institute
Min Lin: Chinese Academy of Agricultural Sciences
Samantha J. O. Hardman: The University of Manchester
Robin Hoeven: The University of Manchester
Michiyo Sakuma: The University of Manchester
Sam Hay: The University of Manchester
David Leys: The University of Manchester
Zihe Rao: Institute of Biophysics, Chinese Academy of Sciences
Aiwu Zhou: Shanghai Jiao Tong University School of Medicine
Qi Cheng: Chinese Academy of Agricultural Sciences
Nigel S. Scrutton: The University of Manchester

Nature, 2019, vol. 574, issue 7780, 722-725

Abstract: Abstract The enzyme protochlorophyllide oxidoreductase (POR) catalyses a light-dependent step in chlorophyll biosynthesis that is essential to photosynthesis and, ultimately, all life on Earth1–3. 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.

Date: 2019
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DOI: 10.1038/s41586-019-1685-2

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