Researchers discover an important role for hydrogen bonding in mitochondrial disease mutation.
Researchers from the Department of Physics, University of Helsinki, Finland and Jagiellonian University, Krakow, Poland found that a subtle hydrogen bonding rearrangement caused by an exercise-intolerance related mitochondrial disease mutation can perturb the normal functioning of the respiratory chain complex III.
Complex III is one of the key enzymes that contributes to energy (ATP) generation in cells.
Energy is generated in the form of ATP in the mitochondria of the cells.
A pathway known as the electron transport chain consists of five enzymes that together synthesize ATP by a complicated movement of electrons and protons.
The third enzyme in this chain is cytochrome bc1 (or complex III), which catalyzes proton pumping in response to electron transfer reactions.
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Researchers discover an important role for hydrogen bonding in mitochondrial disease mutation
