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Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: potential sulfide receptor and storage
Author(s) -
Wang Dandan,
Liu Li,
Wang Hui,
Xu Haoran,
Chen Lei,
Ma Li,
Li Zhengqiang
Publication year - 2016
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.12141
Subject(s) - hemoglobin , chemistry , steric effects , function (biology) , reactivity (psychology) , ligand (biochemistry) , raman spectroscopy , biochemistry , biophysics , receptor , biology , stereochemistry , microbiology and biotechnology , physics , medicine , alternative medicine , pathology , optics
The interaction between H 2 S and Vitreoscilla hemoglobin (VHb) has been studied by UV–Vis and Resonance Raman spectroscopes to confirm the binding between the ligand and the protein. Kinetic constants, k on = 1.2 × 10 5 m −1 ·s −1 and k off = 2.5 × 10 −4 ·s −1 , have been determined and compared with those for mammalian hemoglobins. Density Functional Theory study supports the binding of H 2 S by modeling the configurations of HOMO dispersions. We hypothesized that VHb is involved in H 2 S reception and storage. Different from Lucina pectinata HbI, a typical H 2 S‐binding hemoglobin, VHb, exhibits unusual properties on H 2 S reactivity such as steric constraints playing an important role in modulating H 2 S entry. A distinct mechanism of VHb interaction with H 2 S is supported by studies of variant forms of VHb.