Abstract
The essential role of NAD in the catalytic mechanism of lipoamide dehydrogenase was discovered by Massey and Veeger (1) for the pig heart enzyme and confirmed for the proteins from other species (2). Massey and Veeger concluded from their studies that apart from a role in the catalytic reaction, NAD is bound to an unknown site Y in order to prevent the enzyme against being converted by NADH into the inactive four-equivalent reduced enzyme. The enzyme is only able to exert its physiological function by shuttling between the oxidized and the two-equivalent reduced forms of the enzyme. It was thought that one equivalent reduces the flavin and the second opens a reactive S-S bridge, forming a SH group and a S•-radical.
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References
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Visser, J., Voetberg, H., Veeger, C. (1970). The Role of NAD+ in the Catalytic Mechanism of Lipoamide Dehydrogenase. In: Sund, H. (eds) Pyridine Nucleotide-Dependent Dehydrogenases. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-49974-6_32
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DOI: https://doi.org/10.1007/978-3-642-49974-6_32
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