Redox-induced activation of the proton pump in the respiratory complex I.

Abstract:

:Complex I functions as a redox-linked proton pump in the respiratory chains of mitochondria and bacteria, driven by the reduction of quinone (Q) by NADH. Remarkably, the distance between the Q reduction site and the most distant proton channels extends nearly 200 Å. To elucidate the molecular origin of this long-range coupling, we apply a combination of large-scale molecular simulations and a site-directed mutagenesis experiment of a key residue. In hybrid quantum mechanics/molecular mechanics simulations, we observe that reduction of Q is coupled to its local protonation by the His-38/Asp-139 ion pair and Tyr-87 of subunit Nqo4. Atomistic classical molecular dynamics simulations further suggest that formation of quinol (QH2) triggers rapid dissociation of the anionic Asp-139 toward the membrane domain that couples to conformational changes in a network of conserved charged residues. Site-directed mutagenesis data confirm the importance of Asp-139; upon mutation to asparagine the Q reductase activity is inhibited by 75%. The current results, together with earlier biochemical data, suggest that the proton pumping in complex I is activated by a unique combination of electrostatic and conformational transitions.

authors

Sharma V,Belevich G,Gamiz-Hernandez AP,Róg T,Vattulainen I,Verkhovskaya ML,Wikström M,Hummer G,Kaila VR

doi

10.1073/pnas.1503761112

subject

Has Abstract

pub_date

2015-09-15 00:00:00

pages

11571-6

issue

37

eissn

0027-8424

issn

1091-6490

pii

1503761112

journal_volume

112

pub_type

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