Abstract
Chlorobium vibrioforme f. sp. thiosulfatophilum was shown to oxidize sulphate via substrate phosphorylation involving adenylylsulphate (APS) reductase, ADP-sulphurylase and adenylate kinase. APS reductase was purified 200-fold and shown to be a flavoprotein of molecular weight 1·8 × 105, containing 1 mol flavin adenine dinucleotide (FAD), 4–6 mol non-haem iron and 6–8 mol labile sulphide (mol enzyme)−1. Substrate inhibition of the enzyme was observed when the AMP concentration was above 2 mm. ADP-sulphurylase purified free of adenylate kinase had an apparent K m value for APS of 0·25 mm, which increased with decreasing concentrations of phosphate.
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