Dissected antiporter modules establish minimal proton-conduction elements of the respiratory complex I

Adel Beghiah, Patricia Saura, Sofia Badolato, Hyunho Kim, Johanna Zipf, Dirk Auman, Ana P. Gamiz-Hernandez, Johan Berg, Grant Kemp and Ville R. I. Kaila ()
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Adel Beghiah: Stockholm University
Patricia Saura: Stockholm University
Sofia Badolato: Stockholm University
Hyunho Kim: Stockholm University
Johanna Zipf: Stockholm University
Dirk Auman: Stockholm University
Ana P. Gamiz-Hernandez: Stockholm University
Johan Berg: Stockholm University
Grant Kemp: Stockholm University
Ville R. I. Kaila: Stockholm University

Nature Communications, 2024, vol. 15, issue 1, 1-14

Abstract: Abstract The respiratory Complex I is a highly intricate redox-driven proton pump that powers oxidative phosphorylation across all domains of life. Yet, despite major efforts in recent decades, its long-range energy transduction principles remain highly debated. We create here minimal proton-conducting membrane modules by engineering and dissecting the key elements of the bacterial Complex I. By combining biophysical, biochemical, and computational experiments, we show that the isolated antiporter-like modules of Complex I comprise all functional elements required for conducting protons across proteoliposome membranes. We find that the rate of proton conduction is controlled by conformational changes of buried ion-pairs that modulate the reaction barriers by electric field effects. The proton conduction is also modulated by bulky residues along the proton channels that are key for establishing a tightly coupled proton pumping machinery in Complex I. Our findings provide direct experimental evidence that the individual antiporter modules are responsible for the proton transport activity of Complex I. On a general level, our findings highlight electrostatic and conformational coupling mechanisms in the modular energy-transduction machinery of Complex I with distinct similarities to other enzymes.

Date: 2024
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DOI: 10.1038/s41467-024-53194-5

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