A dehydrogenase from halophilic bacteria was a flavoprotein with FAD as its prothetic group, and its activity was dependent on the presence of NAD+ or NADP+.We speculate that the electron was tansferred from the substrate to NAD(P)+ bound on the enzyme, then to FAD to reduce the flavin? Could the electrons were directly transferred to NAD(P)+, then to FAD? Is it possibly?