Crystal Structure of a Photosynthetic LH1-RC in Complex with Its Electron Donor HiPIP
Overview
Authors
Affiliations
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.
A Native LH1-RC-HiPIP Supercomplex from an Extremophilic Phototroph.
Tani K, Kanno R, Nagashima K, Kawakami M, Hiwatashi N, Nakata K Commun Biol. 2025; 8(1):42.
PMID: 39799244 PMC: 11724841. DOI: 10.1038/s42003-024-07421-w.
Xin J, Min Z, Yu L, Yuan X, Liu A, Wu W Plant Cell. 2024; 36(10):4212-4233.
PMID: 38299372 PMC: 11635291. DOI: 10.1093/plcell/koae029.
Kis M, Szabo T, Tandori J, Maroti P Photosynth Res. 2023; 159(2-3):261-272.
PMID: 38032488 PMC: 10991045. DOI: 10.1007/s11120-023-01059-1.
AI-driven pan-proteome analyses reveal insights into the biohydrometallurgical properties of .
Li L, Zhou L, Jiang C, Liu Z, Meng D, Luo F Front Microbiol. 2023; 14:1243987.
PMID: 37744906 PMC: 10512742. DOI: 10.3389/fmicb.2023.1243987.
Yu L, Min Z, Liu M, Xin Y, Liu A, Kuang J Plant Commun. 2023; 5(2):100715.
PMID: 37710959 PMC: 10873879. DOI: 10.1016/j.xplc.2023.100715.