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Boiled spinach extracts reversibly inhibit the transhydrogenase activity of ferredoxin-nicotinamide adenine dinucleotide phosphate reductase. The inhibition is competitive with respect to NAD but noncompetitive with respect to NADPH. The inhibitor is most effective at a pH of about 8.0. The inhibitor is characterized as an organic acid but does not appear to be a carbohydrate or phosphoric acid derivative or phosphodoxin. A number of compounds with inhibitory activity have been found. These compounds share the common chemical feature of having a vic-carbonyl gouping and include a number of α-keto acids.
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Fredricks et al. (1969) studied this question.
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