Year: 1969
Type: article
Abstract: Sulfite reductase activity by algal extracts was investigated using reduced methylviologen as a hydrogen donor. Sulfite reductase appears to be widely distributed in various algae, but the enzymatic activity was not detected in the brown algae examined. The addition of phosphate buffer to the reaction mixture caused a marked decrease in activity. Sulfite reductase was partially purified from the autolysate of Porphyra tenera and some properties were studied. The optimal pH was 7.5 to 8.5 in Tris-HGl buffer system. The Km for sulfite was 6.65 × 10−4m. The enzymatic activity was completely inhibited by potassium cyanide at 5 × 10−4m. The enzyme catalyzed the reduction of sulfite to sulfide. Neither NADPH nor NADH acts as a hydrogen donor. However, it was revealed that ferredoxin can act as an electron carrier in sulfite reduction to sulfide in Porphyra extract.
Authors: Eizo Saito, Goro Tamura, Sakae Shinano
Institution: Chiba University
Language: English
Subfield: Agronomy and Crop Science
Domain: Life Sciences
Open Access status: bronze
OpenAlex ID: W1693704704