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.
Organizational Affiliation:
Faculty of Science, Ibaraki University, Mito, Japan.
Photosynthesis Research Center, Key Laboratory of Photobiology, Institute of Botany, Chinese Academy of Sciences, Beijing, China. longer@ibcas.ac.cn.
Department of Microbiology, Southern Illinois University, Carbondale, IL, USA.
Department of Agrobioscience, Graduate School of Agriculture, Kobe University, Nada, Kobe, Japan. ykimura@people.kobe-u.ac.jp.
Faculty of Science, Ibaraki University, Mito, Japan. wang@ml.ibaraki.ac.jp.
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