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• W2296975721 startingPage "1132" @default.
• W2296975721 abstract "The interaction between H2S 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, kon = 1.2 × 105 m−1·s−1 and koff = 2.5 × 10−4·s−1, have been determined and compared with those for mammalian hemoglobins. Density Functional Theory study supports the binding of H2S by modeling the configurations of HOMO dispersions. We hypothesized that VHb is involved in H2S reception and storage. Different from Lucina pectinata HbI, a typical H2S-binding hemoglobin, VHb, exhibits unusual properties on H2S reactivity such as steric constraints playing an important role in modulating H2S entry. A distinct mechanism of VHb interaction with H2S is supported by studies of variant forms of VHb." @default.
• W2296975721 created "2016-06-24" @default.
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• W2296975721 date "2016-03-31" @default.
• W2296975721 modified "2023-10-16" @default.
• W2296975721 title "Clues for discovering a new biological function of<i>Vitreoscilla</i>hemoglobin in organisms: potential sulfide receptor and storage" @default.
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• W2296975721 doi "https://doi.org/10.1002/1873-3468.12141" @default.
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