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Cryo-EM structure of a photosystem I variant containing an unusual plastoquinone derivative in its electron transfer chain

Year: 2024
Type: article
Abstract: Photosystem I (PS I) is a light-driven oxidoreductase responsible for converting photons into chemical bond energy. Its application for renewable energy was revolutionized by the creation of the MenB deletion (Δ menB ) variant in the cyanobacterium Synechocystis sp. PCC 6803, in which phylloquinone is replaced by plastoquinone-9 with a low binding affinity. This permits its exchange with exogenous quinones covalently coupled to dihydrogen catalysts that bind with high affinity, thereby converting PS I into a stable solar fuel catalyst. Here, we reveal the 2.03-Å-resolution cryo-EM structure of a recent MenB variant of PS I. The quinones and their binding environment are analyzed in the context of previous biophysical data, thereby enabling a protocol to solve future PS I hybrids and constructs from this genetically tractable cyanobacterium.
DOI: 10.1126/sciadv.adp4937
Authors: Christopher J. Gisriel, Vasily Kurashov, David F. Iwig, Brandon P. Russell, David J. Vinyard, Gary W. Brudvig, John H. Golbeck, K. V. Lakshmi
Institutions: University of Wisconsin–Madison, Yale University, Pennsylvania State University, Howard Hughes Medical Institute, Louisiana State University, Rensselaer Polytechnic Institute
Language: English
Open Access status: gold
Estimated APC paid: $4,500
Funders: U.S. Department of Energy, Yale University, National Institutes of Health, Office of Science, National Institute of General Medical Sciences, Basic Energy Sciences
Awards: ELUCIDATING THE PRINCIPLES THAT CONTROL PROTON-COUPLED ELECTTRON TRANSFER..., G4531288807, ASSEMBLY OF THE PHOTOSYSTEM II REACTION CENTER, High-throughput electron cryo-microscope, CAROTENOID FUNCTION IN NATURAL PHOTOSYNTHETIC SYSTEMS, THE TYPE I HOMODIMERIC REACTION CENTER IN HELIOBACTERIUM MODESTICALDUM
OpenAlex ID: W4404840062
FWCI: 0.462
Cites: 49
Cited by: 4
Related to: 10