Resonance Raman studies and structure of a sulfide complex of methemerythrin

Biochemistry
S M FreierI M Klotz

Abstract

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.

References

Dec 1, 1980·Archives of Biochemistry and Biophysics·S M FreierI M Klotz

Citations

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Related Concepts

Raman Optical Activity Spectroscopy
Sulfides
Ferric Compounds
Metalloproteins
Plasma Protein Binding Capacity
Thioethers
Hemerythrin
Spectrophotometry
Iron-Sulfur Proteins
Hydrogen-Ion Concentration

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