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Default 1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin

1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin.

Related Articles 1H-NMR and EPR studies on met-azido and met-imidazole Dolabella auricularia myoglobin.

Biochim Biophys Acta. 1995 Apr 27;1248(2):149-58

Authors: Yamamoto Y, Suzuki T, Hori H

Met-azido and met-imidazole forms of the myoglobin from the mollusc Dolabella auricularia have been studied by 1H-NMR and EPR spectroscopy. In the mollusc myoglobin, in which His-E7 is replaced by Val, the guanidino group of Arg-E10 serves as an alternative hydrogen-bond donor to the bound ligand. Therefore, the guanidino group of Arg-E10 plays similar roles in ligand stabilization to that the His-E7 imidazole does in most vertebrate myoglobins. Differences in both the structural and electronic properties between Arg and His side chains largely affect the stability of met-azido and met-imidazole forms of the protein. Due to a weak stabilization by Arg-E10, the bound-N3- ligand is replaced by OH- at higher pH, although it is stable at neutral and acidic pH. In the absence of the hydrogen-bonding interaction, Fe-bound imidazole in met-imidazole Dolabella myoglobin is only stable at neutral pH and is removed at acidic pH and replaced by OH- at basic pH. The temperature study also revealed that the bound imidazole is replaced by OH- at higher temperature. These results confirm that the presence of steric hindrance between these bulky ligands and the long and bulky side chain of Arg-E10 in the distal pocket of the mollusc myoglobin. Thus steric effects contribute significantly to the stability of exogenous ligand in the distal pocket of myoglobin.

PMID: 7748897 [PubMed - indexed for MEDLINE]



Source: PubMed
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