Abstract
When the photoheterotroph, Rhodospirillum rubrum, was grown in the light, ferredoxin was excreted from the cells in a significant amount, as well as hydrogenase. The extracellular ferredoxin was purified to a homogeneous state. The molecular weight was approximately 9, 000, and the oxidation-reduction mid-potential was -0.29V (n=1) at pH 7.0 and 25°C. The amino acid composition was different from those of the intracellular ferredoxins, which were already known. The contents of non-heme iron and acid-labile sulfur were 10.6 and 7.9 mol/mol protein, respectively. The extracellular hydrogenase catalyzed the evolution of hydrogen gas from the ferredoxin in the reduced form. The Km for the ferredoxin was 4.1 μM, one-seven hundredth as low as that for methyl viologen. There is a possibility that hydrogenase here were functional for evolution of hydrogen gas outside the cells.
