Abstract
The light-dependent transhydrogenase system of Rhodopseudomonas spheroides can be resolved into a soluble fraction and a chromatophore membrane fraction. The soluble fraction was fractionated with ammonium sulfate, 3 m urea, DE-52 cellulose chromatography, and acrylamide gel electrophoresis and yielded a single protein factor which stimulated light-dependent transhydrogenase activity when added to chromatophores devoid of such activity. It has a molecular weight of approximately 4000–7000, and has a high content of glycine, alanine, glutamic acid, and aspartic acid. The N-terminus amino acid is tryptophan. The factor is heat sensitive and rapidly loses activity upon storage at 4 °C, but is stable at this temperature for about 120 hr if stored in buffer containing 15 μ m DTT. It contains sulfhydryl groups that may be essential for activity.
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