Sulfur-oxidizing enzyme of Ferrobacillus ferrooxidans (Thiobacillus ferrooxidans)

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Abstract
The sulfur-oxidizing enzyme was purified about 15-fold from sulfur-grown Ferrobacillus ferrooxidans. The enzyme has a pH optimum of 7.8 and requires both elemental sulfur and reduced glutathione (GSH); however, a glutathione–polysulfide complex could also serve as substrate. The Km for GSH was determined to be 2 × 10−3 M. Non-heme iron and labile sulfide were present in the enzyme preparation, and sulfite was found to be the end product of the reaction.

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