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• W4386918152 abstract "How does a single amino acid mutation occurring in the blinding disease, Leber's hereditary optic neuropathy (LHON), impair electron shuttling in mitochondria? We investigated changes induced by the m.3460 G>A mutation in mitochondrial protein ND1 using the tools of Molecular Dynamics and Free Energy Perturbation simulations, with the goal of determining the mechanism by which this mutation affects mitochondrial function. A recent analysis suggested that the mutation's replacement of alanine A52 with a threonine perturbs the stability of a region where binding of the electron shuttling protein, Coenzyme Q10, occurs. We found two functionally opposing changes involving the role of Coenzyme Q10. The first showed that quantum electron transfer from the terminal Fe/S complex, N2, to the Coenzyme Q10 headgroup, docked in its binding pocket, is enhanced. However, this positive adjustment is overshadowed by our finding that the mobility of Coenzyme Q10 in its oxidized and reduced states, entering and exiting its binding pocket, is disrupted by the mutation in a manner that leads to conditions promoting the generation of reactive oxygen species. An increase in reactive oxygen species caused by the LHON mutation has been proposed to be responsible for this optic neuropathy." @default.
• W4386918152 created "2023-09-22" @default.
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• W4386918152 date "2023-09-21" @default.
• W4386918152 modified "2023-10-17" @default.
• W4386918152 title "Coenzyme Q10 trapping in mitochondrial complex I underlies Leber’s hereditary optic neuropathy" @default.
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• W4386918152 doi "https://doi.org/10.1073/pnas.2304884120" @default.
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• W4386918152 hasPublicationYear "2023" @default.
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