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NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin

Yamamoto, Yasuhiko ; Suzuki, Tomohiko

Biochimica et biophysica acta, 1993-06, Vol.1163 (3), p.287-296 [Periódico revisado por pares]

Amsterdam: Elsevier B.V

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Título:
NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin
Autor: Yamamoto, Yasuhiko ; Suzuki, Tomohiko
Assuntos: Analytical, structural and metabolic biochemistry ; Animals ; Binding Sites ; Biological and medical sciences ; Dolabella auricularia ; Fundamental and applied biological sciences. Psychology ; Heme ; Heme - chemistry ; Heme electronic structure ; Hemoproteins ; Hot Temperature ; Hydrogen-Ion Concentration ; Hypeffine shift ; Magnetic Resonance Spectroscopy ; Marine ; Metalloproteins ; Metmyoglobin - analogs & derivatives ; Metmyoglobin - chemistry ; Molecular Conformation ; Mollusca - chemistry ; Myoglobin ; Nitrogen Isotopes ; NMR ; Nuclear Overhauser effect ; Proteins
É parte de: Biochimica et biophysica acta, 1993-06, Vol.1163 (3), p.287-296
Notas: ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
Descrição: The molecular and electronic structure of the active site of the cyanide-ligated ferric complex of the myoglobin from the mollusc Dolabella auricularia has been investigated using NMR. Analysis of nuclear Overhauser effects has revealed that the correlation times for the internal motion of the heme propionate α-CH 2 and β-CH 2 groups at ambient temperature are about 5 and 4 ns, respectively. These correlation times indicate that the terminal carboxylate groups of both the heme propionates are not bound to the protein via salt bridges. Although the absence of the propionate-protein interaction does not influence the equilibrium population of the two heme orientational isomers involving rotation about the α-μ-meso axis, it allows the heme to rotate about the iron-His bond in the active site of the myoglobin. Such rotational motion of the heme resulted in an anomalous temperature-dependence of the heme methyl-proton hyperfine shift. Thus the present myoglobin studies provide the first example demonstrating the rotation of the heme about the iron-His bond in native myoglobin.
Editor: Amsterdam: Elsevier B.V
Idioma: Inglês

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NMR study of the molecular and electronic structure of the heme cavity in Dolabella met-cyano myoglobin

Yamamoto, Yasuhiko ; Suzuki, Tomohiko

Amsterdam: Elsevier B.V

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