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Escherichia coli NADPH-sulfite reductase (SiR) is a 780 kDa multimeric hemoflavoprotein composed of eight α-subunits (SiR-FP) and four β-subunits (SiR-HP) that catalyses the six electron reduction of sulfite to sulfide. Each β-subunit contains a Fe4S4 cluster and a siroheme, and each α-subunit binds one FAD and one FMN as prosthetic groups. The FAD gets electrons from NADPH, and the FMN transfers...
The flavoprotein component (SiR-FP) of the sulfite reductase of E. coli is an octamer of the 66 kDa α subunit. It was shown to be cleaved in two peptide fragments. The 23 kDa fragment has been purified as a polymer of 8-10 subunits. It corresponds to the N-terminal part of the native protein and was shown to contain essentially FMN as cofactor. The 43 kDa fragment is monomeric. It contains exclusively...
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