Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
Volume 1860, Issue 3, Pages 224-232Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2018.11.004
Keywords
Molecular dynamics simulations; Lipid-protein interactions; Proton pumping; Energy transduction
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Funding
- Academy of Finland [294652]
- University of Helsinki
- Sigrid Juselius Foundation
- Magnus Ehrnrooth Foundation
- Academy of Finland (AKA) [294652, 294652] Funding Source: Academy of Finland (AKA)
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Mitochondrial cytochrome c oxidase couples the reduction of oxygen to proton pumping. Despite an overall good understanding of its molecular mechanism, the role of cardiolipin in protein function is not understood. Here, we have studied the cardiolipin-protein interactions in a dynamic context by means of atomistic molecular dynamics simulations performed on the entire structure of monomeric and dimeric forms of the enzyme. Several microseconds of simulation data reveal that the crystallographic cardiolipin molecules that glue two monomers together bind weakly in hybrid and single-component lipid bilayers and dissociate rapidly. Atomistic simulations performed in the absence of tightly bound cardiolipin molecules strongly perturb the structural integrity of subunits III and Vila, thereby highlighting an indispensable nature of lipid-protein interactions in enzyme function such as proton uptake and oxygen channeling. Our results demonstrate the strength of molecular simulations in providing direct atomic description of lipid-protein processes that are difficult to achieve experimentally.
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