Importance of the iron–sulfur component and of the siroheme modification in the resting state of sulfite reductase
The active site of sulfite reductase (SiR) consists of an unusual siroheme–Fe4S4 assembly coupled via a cysteinate sulfur, and serves for multi-electron reduction reactions. Clear explanations have not been demonstrated for the reasons behind the choice of siroheme (vs. other types of heme) or for the single-atom coupling to an Fe4S4 center (as opposed to simple adjacency or to coupling via chains