Multiple conformations at functional site of hemerythrin: Evidence from resonance Raman spectra
AUTOR(ES)
Duff, Lori L.
RESUMO
Resonance Raman spectra were obtained for monomeric oxymyohemerythrin and for the azide, thiocyanate, cyanate, cyanide, and fluoride adducts of metmyohemerythrin. The internal ligand vibrations in these complexes appear at essentially the same frequencies as those in the corresponding complexes of octameric hemerythrin. Likewise the Fe—O frequencies in H216O do not depend on quaternary structure of the protein. The anionic adducts fall into two classes in regard to isotope exchange behavior in H218O. They also manifest a novel photochemical transformation from one class of exchange behavior to the other. It seems evident that the functional site in hemerythrin exists in at least two different conformational states and that irradiation can stimulate isotope exchange in the exchange-resistant form.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=319743Documentos Relacionados
- Resonance Raman Studies of the Electronic State of Oxygen in Hemerythrin
- Resonance raman spectra of manganese (III) tetraphenylporphin halides.
- Resonance Raman spectra of bacteriorhodopsin's primary photoproduct: evidence for a distorted 13-cis retinal chromophore.
- Resonance Raman detection of structural dynamics at the active site in hemoglobin.
- RAMAN SPECTRA FROM ACETONE
