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• W2088144234 startingPage "15919" @default.
• W2088144234 abstract "This study explores different UV wavelengths for the resonant Raman excitation of hemoglobin in its two affinity states (T and R). Changes in the T − R difference spectra as a function of excitation wavelength are reported and discussed in context with the excitation profiles of UV resonance Raman bands in the T and the R states. Excitation with 220 nm results in difference signals of the phenylalanine modes F8a and F8b and changes in tryptophan modes associated with the tryptophan residues α14/β15 in the difference spectra. To explore the time-dependent behavior of these changes, we conducted pump−probe experiments and used 220 nm excitation to monitor differences between the photocycle intermediates and HbCO. We found differences in the F8a and F8b modes as early as 40 ns after deligation. These results suggest that phenylalanine residues in close proximity of the heme are probed. In addition, a negative band for the W3 component associated with the α14/β15 tryptophan residues between UVRR spectra of the T and the R states suggests differences in hydrogen bonding of the internal tryptophan residues." @default.
• W2088144234 created "2016-06-24" @default.
• W2088144234 creator A5033485882 @default.
• W2088144234 creator A5070326580 @default.
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• W2088144234 date "2004-09-14" @default.
• W2088144234 modified "2023-10-16" @default.
• W2088144234 title "Time-Resolved Resonance Raman Study of HbA with 220 nm Excitation: Probing Phenylalanine" @default.
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• W2088144234 doi "https://doi.org/10.1021/jp047848k" @default.
• W2088144234 hasPublicationYear "2004" @default.
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