Resonance raman spectroscopy of iron (3)--ovotransferrin and iron (3)--human serum transferrin |
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Authors: | Y Tomimatsu S Kint J R Scherer |
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Institution: | Western Regional Research Center, Agricultural Research Service, U.S. Department of Agriculture, Berkeley, California 94710 USA |
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Abstract: | We report the resonance Raman spectra in the frequency range 300–1800 cm?1 of Fe (III)-ovotransferrin and Fe (III)-human serum transferrin in aqueous solution at about 10?4M protein concentration. This is the first observation of resonance Raman scattering ascribable to amino acid ligand vibrational modes of a nonheme iron protein. The resonance Raman spectra of the transferrins are similar except that the resonance band near 1270 cm?1 is shifted to a higher frequency for Fe(III)-human serum transferrin than that for Fe(III)-ovotransferrin. The resonance Raman bands observed near 1170, 1270, 1500 and 1600 cm?1 may reflect resonance enhancement of p-hydroxy-phenyl frequencies of tyrosine residues and/or imidazolium frequencies of histidine residues. |
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