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Differences in the heme environment of soybean leg hemo globin components shown by proton nmr spectroscopy






Biochimica et Biophysica Acta 700(2): 171-177

Differences in the heme environment of soybean leg hemo globin components shown by proton nmr spectroscopy

1H-NMR spectra were recorded for the cyanide complexes of homogeneous soybean ferric leghemoglobin components a, c1, c3 and a mixture of components c2 + c3, isolated by anion-exchange chromatography at pH 5.2. Small chemical shift differences are observed for the heme resonances in the spectra of the different components, indicating small differences in heme electronic structure which are attributed to substitutions among the heme contact residues. The heme environment is closely but not exactly conserved in the various soybean leghemoglobins and this might be reflected in their biological functions. The chemical shifts of the heme resonances of the component leghemoglobins in an unresolved mixture which was not subjected to low-pH chromatography are identical to those of the components a, c1, c2 and c3 isolated at pH 5.2. The 4 major leghemoglobin components are therefore not artifacts of the separation procedure.

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Accession: 005151301



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