期刊
JOURNAL OF INORGANIC BIOCHEMISTRY
卷 179, 期 -, 页码 32-39出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.jinorgbio.2017.10.015
关键词
Hemoglobin; Myoglobin; Hydrogen sulfide; Sulfoferryl; Hexachloroiridate; Protein adduct
资金
- Romanian National Authority for Scientific Research and Innovation (CNCS - UEFISCDI) [PN-II-ID-PCE-2012-4-0488]
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 pH 9.5, 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 beta-chain is truncated at Tyr144.
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