Abstract
A mechanism is postulated for adenylyl sulfate (APS) reductase, considered as the oxidation of sulfite to the level of sulfate (APS), which involves three steps in the absence of an added electron acceptor. The first step involves the reversible association of sulfite with enzyme-bound FAD to form a flavin-sulfite adduct; the second, a transfer of the sulfur moiety from FAD to a mononucleotide acceptor to yield the corresponding nucleotide 5′-phosphosulfate; and the third, the internal reduction of an as yet unknown chromophore to yield oxidized FAD.
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