Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

Tomoaki Kawakami, Long-Jiang Yu (), Tai Liang, Koudai Okazaki, Michael T. Madigan, Yukihiro Kimura () and Zheng-Yu Wang-Otomo ()
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Tomoaki Kawakami: Ibaraki University
Long-Jiang Yu: Chinese Academy of Sciences
Tai Liang: Ibaraki University
Koudai Okazaki: Ibaraki University
Michael T. Madigan: Southern Illinois University
Yukihiro Kimura: Kobe University
Zheng-Yu Wang-Otomo: Ibaraki University

Nature Communications, 2021, vol. 12, issue 1, 1-8

Abstract: Abstract Photosynthetic electron transfers occur through multiple components ranging from small soluble proteins to large integral membrane protein complexes. Co-crystallization of a bacterial photosynthetic electron transfer complex that employs weak hydrophobic interactions was achieved by using high-molar-ratio mixtures of a soluble donor protein (high-potential iron-sulfur protein, HiPIP) with a membrane-embedded acceptor protein (reaction center, RC) at acidic pH. The structure of the co-complex offers a snapshot of a transient bioenergetic event and revealed a molecular basis for thermodynamically unfavorable interprotein electron tunneling. HiPIP binds to the surface of the tetraheme cytochrome subunit in the light-harvesting (LH1) complex-associated RC in close proximity to the low-potential heme-1 group. The binding interface between the two proteins is primarily formed by uncharged residues and is characterized by hydrophobic features. This co-crystal structure provides a model for the detailed study of long-range trans-protein electron tunneling pathways in biological systems.

Date: 2021
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DOI: 10.1038/s41467-021-21397-9

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