Resonance Raman studies of Escherichia coli sulfite reductase hemoprotein. 3. Bound ligand vibrational modes.

The vibrations of the bound diatomic heme ligands CO, CN-, and NO are investigated by resonance Raman spectroscopy in various redox states of Escherichia coli sulfite reductase hemoprotein, and assignments are generated by use of isotopically labeled ligands. For the fully reduced CO complex (ferrous siroheme, reduced Fe4S4 cluster) at room temperature, nu CO is observed at 1904 cm-1, shifting to 1920 cm-1 upon oxidation of the cluster. The corresponding delta FeCO modes are identified at 574 and 566 cm-1, respectively, by virtue of the zigzag pattern of their isotopic shifts. In frozen solution, two species are observed for the cluster-oxidized state, with nu CO at 1910 and 1936 cm-1 and nu FeC at 532 and 504 cm-1, respectively; nu FeC for the fully reduced species is identified at 526 cm-1 in the frozen state. For the ferrous siroheme-NO complex (cluster oxidized), nu NO is identified at 1555 cm-1 in frozen solution and a low-frequency mode is identified at 558 cm-1; this stretching mode is significantly lower than that observed in Mb-NO. For the ferric siroheme cyanide complexes evidence of two ligand-bonding forms is observed, with modes at 451/390 and 451/352 cm-1; they are distinguished by a reversal of the isotopic shift patterns of the upper and lower modes and could arise from a linear and a bent Fe-C unit, respectively. For the ferrous siroheme cyanide complex isotope-sensitive modes observed at 495 and 452 cm-1 are assigned to the FeCN- bending and FeC stretching vibrations, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)