Catalytic activity of the chromophore of desulfoviridin, sirohydrochlorin, in sulfite reduction in the presence of iron.

Sirohydrochlorin chromophore prepared by acetone/HCl treatment of desulfoviridin, the sulfite reductase from Desulfovibrio, catalyzed the reduction of sulfite to sulfide and thiosulfate in equimolar amounts when coupled with a hydrogen-hydrogenase-methyl viologen system. This activity was manifested at acidic pH and increased exponentially with decrease in pH. The Km value for sulfite was nearly 10 times that of desulfoviridin. Inorganic iron was necessary for the reduction, since inactivation occurred on passage through a Sephadex LH-20 column or in the presence of 2,2'-bipyridine, and reactivation was observed on adding iron. The chromophore catalyzed the reduction of dithionite and hyroxylamine.