Resonance Raman studies and structure of a sulfide complex of methemerythrin.
The complex of sulfide and methemerythrin has been characterized by resonance Raman spectroscopy. At pH 8.0 the complex contains two irons and one S2- at the active site. The resonance Raman spectrum of the sulfidomethemerythrin complex contains only one vibration, at 444 cm-1. This vibration is assigned to an iron-sulfide stretch. The possibility that sulfidomethemerythrin contains a mu-sulfido bridge. FeIII-S2-FeIII, analogous to the proposed mu-oxo bridge in azidomethemerythrin is discussed.
D000818:Animals; D005290:Ferric Compounds; D006422:Hemerythrin; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000032:analysis; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D009348:Nematoda / Q000032:analysis*; D011485:Protein Binding; D013053:Spectrophotometry; D013059:Spectrum Analysis, Raman; D013440:Sulfides / Q000032:analysis
D005290:Ferric Compounds; D006422:Hemerythrin; D007506:Iron-Sulfur Proteins; D008667:Metalloproteins; D013440:Sulfides; D007501:Iron