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• W2080815075 startingPage "12988" @default.
• W2080815075 abstract "Solution 1H NMR spectroscopy has been used to determine the relative strengths (covalency) of the two axial His−Fe bonds in paramagnetic, S = 1/2, human met-cytoglobin. The sequence specific assignments of crucial portions of the proximal and distal helices, together with the magnitude of hyperfine shifts and paramagnetic relaxation, establish that His81 and His113, at the canonical positions E7 and F8 in the myoglobin fold, respectively, are ligated to the iron. The characterized complex (∼90%) in solution has protohemin oriented as in crystals, with the remaining ∼10% exhibiting the hemin orientation rotated 180° about the α-, γ-meso axis. No evidence could be obtained for any five-coordinate complex (<1%) in equilibrium with the six-coordinate complexes. Extensive sequence-specific assignments on other dipolar shifted helical fragments and loops, together with available alternate crystal coordinates for the complex, allowed the robust determination of the orientation and anisotropies of the paramagnetic susceptibility tensor. The tilt of the major axis is controlled by the His−Fe−His vector, and the rhombic axes are controlled by the mean of the imidazole orientations for the two His. The anisotropy of the paramagnetic susceptibility tensor allowed the quantitative factoring of the hyperfine shifts for the two axial His to reveal an indistinguishable pattern and magnitudes of the contact shifts or π spin densities, and hence, indistinguishable Fe-imidazole covalency for both Fe−His bonds." @default.
• W2080815075 created "2016-06-24" @default.
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• W2080815075 date "2006-09-07" @default.
• W2080815075 modified "2023-09-27" @default.
• W2080815075 title "Solution ¹H NMR Characterization of the Axial Bonding of the Two His in Oxidized Human Cytoglobin" @default.
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• W2080815075 doi "https://doi.org/10.1021/ja063330d" @default.
• W2080815075 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2566969" @default.
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