Rotational barriers of 1,3-substituted pyridines and benzenes as models for the NAD+/NADH coenzyme

Kinetic and modelling studies of NAD+ and poly(ethylene glycol)-bound NAD+ in horse liver alcohol dehydrogenase

“…[20]. This resulted in a rotational barrier of 12.6 kJ mol-~ around the C3--C7 bond of the nicotinamide moiety of the free coenzyme.…”

“…In the past we have used a molecular mechanics approach to study in detail the interactions of the coenzyme NAD + and a number of analogues in the active site of HLADH, in order to understand the essential factors involved in the productive binding between coenzyme and apo-enzyme [17][18][19][20]. In this paper we present the results of detailed kinetic studies on HLADH with PEG-NAD ÷ as coenzyme, and an extension of our modelling studies including molecular mechanics (MM) and dynamics (MD), to rationalize the kinetic data obtained.…”