Two artificial coenzymes based on a triazine dye template, Blue N-3 and Nap I, have previously been shown to display coenzymic activity with horse liver alcohol dehydrogenase (HLADH).(1-3) This paper describes the design, synthesis, and properties of a number of new analogues aimed at probing the effects of various alternative groups in the terminal position distal from the active nicotinamide group (Figure 1). W-visible absorption spectroscopy was used to demonstrate that the coenzyme analogues bind to HLADH, and that binding is competitive with the binding of NADH. The coenzymic activities of the new analogues with HLADH and butan-1-ol at pH 7.5 were compared to Nap 1. All of the new analogues exhibited turnover in the enzymic reaction; thus, it appears that the enzyme can tolerate several groups in the terminal position distal from the nicotinamide group while still retaining catalytic activity.