Abstract
The pyridine nucleotide transhydrogenase of Escherichia coli consists of two types of subunit (α: M r 53 906; β: M r 48 667). The purified and membrane-bound enzymes were crosslinked with a series of bifunctional crosslinking agents and by catalyzing the formation of inter-chain disulfides in the presence of cupric 1,10-phenanthrolinate. Crosslinked dimers α 2, αβ and β 2, and the trimer α 2 β were obtained. A small amount of tetramer, probably α 2 β 2, was also formed. Radiation inactivation was used to determine the molecular size of the transhydrogenase. The radiation inactivation size (217 000) and chemical crosslinking are consistent with the structure ( M r 205 146) being the oligomer that is responsible for biological activity.
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