A New Way To Understand Quaternary Structure Changes of Hemoglobin upon Ligand Binding On the Basis of UV-Resonance Raman Evaluation of Intersubunit Interactions

The single residue vibrational spectra of tryptophan (Trp) and tyrosine (Tyr) residues in human adult hemoglobin (HbA), which play important roles in cooperative oxygen binding, were determined for the deoxy and CO-bound forms by applying UV resonance Raman spectroscopy to various variant Hbs. It wa...

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Veröffentlicht in:	Journal of the American Chemical Society 2011-07, Vol.133 (26), p.10101-10110
Hauptverfasser:	Nagatomo, Shigenori, Nagai, Masako, Kitagawa, Teizo
Format:	Artikel
Sprache:	eng
Schlagworte:	Carbon Monoxide - metabolism Hemoglobins - chemistry Hemoglobins - genetics Hemoglobins - metabolism Humans Iron - metabolism Ligands Models, Molecular Mutation Nickel - metabolism Protein Binding Protein Structure, Quaternary - drug effects Protein Subunits - chemistry Protein Subunits - genetics Protein Subunits - metabolism Spectrophotometry, Ultraviolet Spectrum Analysis, Raman
Online-Zugang:	Volltext
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