title: Clues for discovering a new biological function of Vitreoscilla hemoglobin in organisms: potential sulfide receptor and storage.
abstract: The interaction between H2 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, kon = 1.2 × 10(5) 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 H2 S by modeling the configurations of HOMO dispersions. We hypothesized that VHb is involved in H2 S reception and storage. Different from Lucina pectinata HbI, a typical H2 S-binding hemoglobin, VHb, exhibits unusual properties on H2 S reactivity such as steric constraints playing an important role in modulating H2 S entry. A distinct mechanism of VHb interaction with H2 S is supported by studies of variant forms of VHb.
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun, Jilin Province, China.
authors.forename: Dandan
authors.initials: D
authors.lastname: Wang
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun, Jilin Province, China.
authors.forename: Li
authors.initials: L
authors.lastname: Liu
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun, Jilin Province, China.
authors.forename: Hui
authors.initials: H
authors.lastname: Wang
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun, Jilin Province, China.
authors.forename: Haoran
authors.initials: H
authors.lastname: Xu
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun, Jilin Province, China.
authors.forename: Lei
authors.initials: L
authors.lastname: Chen
authors.affiliation: Department of Physics Georgia Southern University, Statesboro, GA, USA.
authors.forename: Li
authors.initials: L
authors.lastname: Ma
authors.affiliation: Key Laboratory for Molecular Enzymology and Engineering of Ministry of Education, College of Life Science, Jilin University, Changchun, Jilin Province, China.
authors.forename: Zhengqiang
authors.initials: Z
authors.lastname: Li
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D006736:Horses; D006862:Hydrogen Sulfide / Q000378:metabolism; D007700:Kinetics; D008024:Ligands; D008958:Models, Molecular; D050505:Mutant Proteins / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D018035:Receptors, Odorant / Q000378:metabolism*; D016415:Sequence Alignment; D013057:Spectrum Analysis; D013059:Spectrum Analysis, Raman; D034421:Sus scrofa; D054793:Truncated Hemoglobins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D060829:Arthropod Proteins; D001426:Bacterial Proteins; D008024:Ligands; D050505:Mutant Proteins; D018035:Receptors, Odorant; D054793:Truncated Hemoglobins; C078197:sulfide receptor; C082613:hemoglobin protein, Vitreoscilla; D006862:Hydrogen Sulfide
keywords: Resonance Raman spectroscopy; hemoglobin; hydrogen sulfide; stopped-flow technique