Structural determinants for the formation of sulfhemeprotein complexes

Elddie Román-Morales, Ruth Pietri, Brenda Ramos-Santana, Serge N. Vinogradov, Ariel Lewis-Ballester, Juan López-Garriga

Research output: Contribution to journalArticlepeer-review

42 Scopus citations


Several hemoglobins were explored by UV-Vis and resonance Raman spectroscopy to define sulfheme complex formation. Evaluation of these proteins upon the reaction with H 2O 2 or O 2 in the presence of H 2S suggest: (a) the formation of the sulfheme derivate requires a HisE7 residue in the heme distal site with an adequate orientation to form an active ternary complex; (b) that the ternary complex intermediate involves the HisE7, the peroxo or ferryl species, and the H 2S molecule. This moiety precedes and triggers the sulfheme formation.

Original languageEnglish (US)
Pages (from-to)489-492
Number of pages4
JournalBiochemical and Biophysical Research Communications
Issue number4
StatePublished - Oct 1 2010


  • Ferryl species
  • Hemoglobin I (HbI)
  • Histidine (His)
  • Hydrogen peroxide (H O )
  • Hydrogen sulfide (H S)
  • Sulfhemoglobin
  • Sulfmyoglobin

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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