The structure of Photosystem I acclimated to far-red light illuminates an ecologically important acclimation process in photosynthesis

Gisriel, Christopher; Shen, Gaozhong; Kurashov, Vasily; Ho, Ming-Yang; Zhang, Shangji; Williams, Dewight; Golbeck, John H.; Fromme, Petra; Bryant, Donald A.

doi:10.1126/sciadv.aay6415

Title: The structure of Photosystem I acclimated to far-red light illuminates an ecologically important acclimation process in photosynthesis

Journal Article · 01 February 2020 · Science Advances

DOI: https://doi.org/10.1126/sciadv.aay6415 · OSTI ID:1626049

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^[2]; Kurashov, Vasily ^[2];

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^[4]; Williams, Dewight ^[4];

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Arizona State Univ., Mesa, AZ (United States). Biodesign Ctr for Applied Structural Discovery; Arizona State Univ., Mesa, AZ (United States). School of Molecular Sciences
Pennsylvania State Univ., University Park, PA (United States). Dept. of Biochemistry and Molecular Biology
Pennsylvania State Univ., University Park, PA (United States). Dept. of Biochemistry and Molecular Biology; Pennsylvania State Univ., University Park, PA (United States). Intercollege Graduate Program in Plant Biology
Arizona State Univ., Mesa, AZ (United States). Biodesign Ctr for Applied Structural Discovery
Pennsylvania State Univ., University Park, PA (United States). Dept. of Biochemistry and Molecular Biology; Pennsylvania State Univ., University Park, PA (United States). Dept. of Chemistry
Pennsylvania State Univ., University Park, PA (United States). Dept. of Biochemistry and Molecular Biology; Pennsylvania State Univ., University Park, PA (United States). Intercollege Graduate Program in Plant Biology; Montana State Univ., Bozeman, MT (United States). Dept. of Chemistry and Biochemistry

Phototrophic organisms are superbly adapted to different light environments but often must acclimate to challenging competition for visible light wavelengths in their niches. Some cyanobacteria overcome this challenge by expressing paralogous photosynthetic proteins and by synthesizing and incorporating ~8% chlorophyll f into their Photosystem I (PSI) complexes, enabling them to grow under far-red light (FRL). We solved the structure of FRL-acclimated PSI from the cyanobacteriumFischerella thermalisPCC 7521 by single-particle, cryo–electron microscopy to understand its structural and functional differences. Four binding sites occupied by chlorophyll f are proposed. Subtle structural changes enable FRL-adapted PSI to extend light utilization for oxygenic photosynthesis to nearly 800 nm. This structure provides a platform for understanding FRL-driven photosynthesis and illustrates the robustness of adaptive and acclimation mechanisms in nature.

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Research Organization:: Washington Univ., St. Louis, MO (United States)

Sponsoring Organization:: USDOE Office of Science (SC)

Grant/Contract Number:: SC0001035

OSTI ID:: 1626049

Journal Information:: Science Advances, Vol. 6, Issue 6; ISSN 2375-2548

Publisher:: AAASCopyright Statement

Country of Publication:: United States

Language:: English

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