The metal cofactor: Stationary or mobile?
Peter Leon Hagedoorn (TU Delft - BT/Biocatalysis)
Martin Pabst (TU Delft - BT/Environmental Biotechnology)
Ulf Hanefeld (TU Delft - BT/Biocatalysis)
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Abstract
Metal cofactors are essential for catalysis and enable countless conversions in nature. Interestingly, the metal cofactor is not always static but mobile with movements of more than 4 Å. These movements of the metal can have different functions. In the case of the xylose isomerase and medium-chain dehydrogenases, it clearly serves a catalytic purpose. The metal cofactor moves during substrate activation and even during the catalytic turnover. On the other hand, in class II aldolases, the enzymes display resting states and active states depending on the movement of the catalytic metal cofactor. This movement is caused by substrate docking, causing the metal cofactor to take the position essential for catalysis. As these metal movements are found in structurally and mechanistically unrelated enzymes, it has to be expected that this metal movement is more common than currently perceived.
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