Three rate-determining protein roles in photosynthetic O2-evolution addressed by time-resolved experiments on genetically modified photosystems

Sarah M. Mäusle, Gianluca Parisse, Ricardo Assunção, Cristina Santis, Philipp S. Simon, Daniele Narzi, Leonardo Guidoni (), Richard J. Debus () and Holger Dau ()
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Sarah M. Mäusle: Freie Universität Berlin
Gianluca Parisse: University of L’Aquila
Ricardo Assunção: Freie Universität Berlin
Cristina Santis: University of L’Aquila
Philipp S. Simon: Freie Universität Berlin
Daniele Narzi: University of L’Aquila
Leonardo Guidoni: University of L’Aquila
Richard J. Debus: University of California
Holger Dau: Freie Universität Berlin

Nature Communications, 2025, vol. 16, issue 1, 1-17

Abstract: Abstract Light-driven water splitting by plants, algae and cyanobacteria is pivotal for global bioenergetics and biomass formation. A manganese cluster bound to the photosystem II proteins catalyzes the complex reaction at high rate, but the rate-determining factors are insufficiently understood. Here we trace the oxygen-evolution transition by time-resolved polarography and infrared spectroscopy for cyanobacterial photosystems genetically modified at two strategic sites, complemented by computational chemistry. Our results highlight three rate-determining roles of the protein environment of the metal cluster: acceleration of proton-coupled electron transfer, acceleration of substrate-water insertion after O2-formation, and balancing of rate-determining enthalpic and entropic contributions. Whereas in general the substrate-water insertion step may be unresolvable in time-resolved experiments, here it likely becomes traceable because of deceleration by genetic modification. Our results may stimulate new time-resolved experiments on substrate-water insertion in photosynthesis, clarification of enthalpy-entropy compensation in enzyme catalysis, and knowledge-guided development of inorganic catalyst materials.

Date: 2025
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DOI: 10.1038/s41467-025-64513-9

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