title: Comparison of hemerythrins from four species of sipunculids by optical absorption, circular dichroism, fluorescence emission, and resonance Raman spectroscopy.
abstract: Resonance Raman, optical absorption, circular dichroic, and fluorescence emission spectroscopy of hemerythrins from four species of sipunculids (Phascolopsis gouldii, Phascolosoma agassizii, Themiste dyscritium, and Themiste pyroides) reveals no major differences in their active site or tertiary structures. This precludes any change in iron ligands or coodination geometry and makes it unlikely that the active-site structures of P. gouldii and T. dyscritum hemerythrins could be as disparate as indicated by present crystallographic interpretations (Stenkamp, R. E., Sieker, L. C., and Jensen, L. H. (1976), Proc. Natl. Acad. Sci. U.S.A. 73, 349; Klotz, I. M., Klippenstein, G. L., and Hendrickson, W. A. (1976), Science 192, 335). Resonance Raman enhancement profiles of the stretching modes involving coordinated dioxygen maximize with excitation at approximately 525 nm, and correspond to the circular dichroic (CD) transition at approximately 520 nm. For coordinated azide modes in metazidohemerythrins these profiles maximize with excitation at approximately 505 nm corresponding to the 500-nm CD transition. Hemerythrins also possess another resonance Raman peak at approximately 510 cm-1 which show maximum intensity enhancement at approximately 530 nm and this vibration is most likely associated with a permanent iron ligand.
mesh_terms: D000818:Animals; D000845:Annelida / Q000032:analysis*; D001386:Azides; D002942:Circular Dichroism; D006422:Hemerythrin; D008667:Metalloproteins; D010100:Oxygen; D011485:Protein Binding; D011487:Protein Conformation; D013045:Species Specificity; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D013056:Spectrophotometry, Ultraviolet; D013059:Spectrum Analysis, Raman
chemical_list: D001386:Azides; D006422:Hemerythrin; D008667:Metalloproteins; D010100:Oxygen