SUMMARY: Energy-dependent and energy-independent transhydrogenase activities in the membrane particle fraction from were less markedly repressed by amino acids than in . Energy-dependent transhydrogenation of NADP by NADH was driven either by energy from NADH oxidation through the respiratory chain, or from ATP, GTP or ITP but not by CTP, UTP, ADP and adenosine monophosphates. Adenosine monophosphates had little effect on ATP-driven and energy-independent reactions but 5′-AMP and 3′,5′-AMP, like cyanide and sulphide, inhibited the aerobic-driven reaction via an inhibitory effect on the respiratory chain of the organism. Dicyclohexylcarbodi-imide and phosphate inhibited the use of ATP as an energy donor, while carbonyl cyanide--chlorophenylhydrazone discharged the energized state required for energy-dependent transhydrogenation. Washing removed proteins needed for both energy-dependent activities but not for the energy-independent reaction. Re-addition of the “coupling factor” restored the lost activities fully. Coupling factor preparations from this organism and from were interchangeable.


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