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Key role of quinone in the mechanism of respiratory complex I

Biology

Key role of quinone in the mechanism of respiratory complex I

J. Gutiérrez-fernández, K. Kaszuba, et al.

Discover groundbreaking insights into respiratory complex I in this fascinating study by Javier Gutiérrez-Fernández and colleagues. The research reveals how quinone binding, rather than NADH, triggers significant structural changes that are crucial for understanding the energy coupling mechanism in this vital complex.

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Playback language: English
Abstract
This paper investigates the mechanism of respiratory complex I, focusing on the role of quinone. Using X-ray crystallography and cryo-EM, five crystal structures of *T. thermophilus* complex I with NADH or quinone-like compounds, and cryo-EM structures of native states, were determined. Results show quinone binding (not NADH) induces global conformational changes, propagating from the quinone site to proton channels. Analysis suggests quinone binding and chemistry are key to complex I's coupling mechanism.
Publisher
Nature Communications
Published On
Aug 18, 2020
Authors
Javier Gutiérrez-Fernández, Karol Kaszuba, Gurdeep S. Minhas, Rozbeh Baradaran, Margherita Tambalo, David T. Gallagher, Leonid A. Sazanov
Tags
complex I
quinone
NADH
X-ray crystallography
cryo-EM
proton channels
energy coupling

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