Chem. J. Chinese Universities

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Ligand Binding Affinity of Cyanide Complex of Single Mutant F106L Murine Met-Neuroglobin

DU Wei-Hong1,3, YIN Guo-Wei1, LI Yan-Jie2, WEI Qun2, LI Juan3, FANG Wei-Hai3*   

    1. Department of Chemistry, Renmin University of China, Beijing 100872, China;
    2. College of Life Science,
    3. College of Chemistry, Beijing Normal University, Beijing 100875, China
  • Received:2006-11-07 Revised:1900-01-01 Online:2007-08-10 Published:2007-08-10
  • Contact: FANG Wei-Hai

Abstract: Neuroglobin(Ngb), a recently discovered mammalian heme protein, is predominantly expressed in vertebrate brain and retina. The site G5(F106) in protein structure has been proved as one of the key proximal residues in maintenance of heme pocket conformation. Herein, to investigate the attributions of heme pocket structure of Ngb, especially in proximal side, the mutant F106L was implemented in laboratory. Solution 1H NMR method was utilized to study the binding process of exterior ligand CN- to F106L Ngb mutant. The results indicate that in the binding of CN- with NgbF106L a dynamic process exists and the Ngb F106LCN complex could reversibly release CN-, hence the interior His64 might rebind to iron as the sixth ligand. It reveals that the G5 residue in Ngb serves to conservation in partial conformation of heme pocket predominantly. Furthermore, molecular mechanics calculation suggests that proximal residues like G5 and FG5 in Ngb also take an important role in serving for structural stability and controlling the thermodynamics and kinetics of coordination equilibrium of met-neuroglobin with exterior ligand.

Key words: Neuroglobin, Mutant(F106L), Reversible binding, NMR

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