Abstract
Extracts of representative bacterial strains from the various families of photosynthetic prokaryotes are demonstrated to possess significant levels of sulfite reductase [EC 1.8.99.1; hydrogen-sulfide: (acceptor)oxidoreductase] activity with reduced methyl viologen as electron donor, but not NADPH(2). The enzyme is localized primarily in the soluble fraction of the extracts, in contrast to adenylysulfate reductase [EC 1.8.99.2; AMP, sulfite: (acceptor) oxidoreductase], which is bound normally in the membrane fractions of those bacteria in which it is found. Assignment of the sulfite reductase activities to the biosynthetic ("assimilatory") pathway is suggested by levels of specific activity noted and ready solubility.