Structure of cog at the hub of metabolism reveals anti-ageing function

olecules, like glucose, to release energy for use in the body. Found deep inside most human cells in tiny power plants called mitochondria, succinate dehydrogenase plays a key part in this process when oxygen is present. Embedded in the inner membrane of the mitochondria, the enzyme is involved in a system that transfers energy using electrons.

Using the latest X-ray crystallography techniques, Imperial PhD student, Rob Horsfield solved the structure of succinate dehydrogenase. Researchers from the UK, Sweden, the United States and Japan were then able to probe the three-dimensional structure of the protein, to examine how the enzyme releases energy by breaking down a derivative of glucose, succinate, to a smaller molecule fumarate.

To determine what factors influence free radical production, the team compared the structure of succinate dehydrogenase to a similar enzyme, fumarate reductase.

"Until now, it has been unclear why cells preferentially use succinate dehydrogenase in the presence of oxygen and fumarate reductase in its absence to perform the same job," explains Professor Iwata.

"Previous research indicates that fumarate reductase produces 120 times more superoxide than succinate dehydrogenase in the presence of oxygen. Now, we can see why subtle differences between the two structures means that when energy is released from succinate it is not transferred to the next stage of respiration but leaks out, leading to superoxide production."

Professor Iwata added: "Succinate dehydrogenase's structure is far more efficient at handing that energy onto the next stage of respiration. It seems likely that there has been evolutionary pressure for organisms to pick succinate dehydrogenase to limit the damage inflicted on cells by superoxide production."


Contact: Judith H. Moore
Imperial College London

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