Salmonella typhimurium, sulfite reductase

Fig. 46. Comparison of the absorption spectra of wild-type and mutant (cys G-439 and cys 1-68) sulfite reductases from Salmonella typhimurium. Spectra of S. typhi-murium sulfite reductase, cys G-439 NADPH-cytochrome e reductase, and cys 1-68 NADPH-oytoohrome c reductase, each dissolved in 0D5 M potassium phosphate buffer, pH 7.7, containing 0.1 mM EDTA, were read against a blank containing only buffer. The spectrum of each enzyme is presented in terms of its millimolar extinction coefficients, assuming 8 moles of flavin per mole of enzyme. Light broken line, calculated difference spectrum between those of wild-type and cys G enzymes when both enzyme solutions contain equal concentrations of flavin. From Siegel et al. (394).

Ostrowski, J., M.J. Barber, D.C. Rueger, B.E. Miller, L.M. Siegel, and N.M. Kredich (1989). Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase. J. Biol. Chem. 264, 15796-15808. 

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