Fe(III) - Sulfide interaction in globins: Characterization and quest for a putative Fe(IV)-sulfide species

J Inorg Biochem. 2018 Feb:179:32-39. doi: 10.1016/j.jinorgbio.2017.10.015. Epub 2017 Nov 10.

Abstract

The present study reports findings regarding the contrast between H2S interaction with bovine hemoglobin (Hb) and horse heart myoglobin (Mb), in terms of binding and dissociation kinetics, affinities, and mechanism. At pH9.5, oxidation of ferric-sulfide adducts in presence of no free sulfide, using hexachloroiridate as oxidant is examined using stopped-flow UV-vis, EPR, vibrational spectroscopy and mass spectrometry. Oxidation of the ferric-sulfide adduct in such conditions occurs with a putative unstable Fe(IV)-sulfide adduct as intermediate that finally leads to a paramagnetic ferric species with distinct EPR features. As detected by MS spectrometry, this final species appears to be a truncated form of globin at a distinct Tyr. In case of Hb, only β-chain is truncated at Tyr144.

Keywords: Hemoglobin; Hexachloroiridate; Hydrogen sulfide; Myoglobin; Protein adduct; Sulfoferryl.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cattle
  • Hemoglobins / chemistry*
  • Horses
  • Hydrogen Sulfide / chemistry*
  • Hydrogen-Ion Concentration
  • Iron / chemistry*
  • Kinetics
  • Myocardium / chemistry
  • Myoglobin / chemistry*
  • Oxidation-Reduction

Substances

  • Hemoglobins
  • Myoglobin
  • Iron
  • Hydrogen Sulfide