Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: Potential sulfide receptor and storage

Dandan Wang; Li Liu; Hui Wang; Haoran Xu; Lei Chen; Li Ma; Zhengqiang Li

doi:10.1002/1873-3468.12141

Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: Potential sulfide receptor and storage

Dandan Wang, Li Liu, Hui Wang, Haoran Xu, Lei Chen, Li Ma, Zhengqiang Li

Biochemistry, Chemistry & Physics

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

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, k_on = 1.2 × 10⁵ 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 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.

Original language	English
Pages (from-to)	1132-1142
Number of pages	11
Journal	FEBS Letters
Volume	590
Issue number	8
DOIs	https://doi.org/10.1002/1873-3468.12141
State	Published - Apr 1 2016

Scopus Subject Areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Keywords

hemoglobin
hydrogen sulfide
Resonance Raman spectroscopy
stopped-flow technique

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10.1002/1873-3468.12141

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title = "Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: Potential sulfide receptor and storage",

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.",

keywords = "hemoglobin, hydrogen sulfide, Resonance Raman spectroscopy, stopped-flow technique",

author = "Dandan Wang and Li Liu and Hui Wang and Haoran Xu and Lei Chen and Li Ma and Zhengqiang Li",

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doi = "10.1002/1873-3468.12141",

language = "English",

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T1 - Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms

T2 - Potential sulfide receptor and storage

AU - Wang, Dandan

AU - Liu, Li

AU - Wang, Hui

AU - Xu, Haoran

AU - Chen, Lei

AU - Ma, Li

AU - Li, Zhengqiang

PY - 2016/4/1

Y1 - 2016/4/1

N2 - 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.

AB - 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.

KW - hemoglobin

KW - hydrogen sulfide

KW - Resonance Raman spectroscopy

KW - stopped-flow technique

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JO - FEBS Letters

JF - FEBS Letters

IS - 8

ER -

Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: Potential sulfide receptor and storage

Abstract

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Keywords

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