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- W2335172489 endingPage "10110" @default.
- W2335172489 startingPage "10101" @default.
- W2335172489 abstract "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 was found that Trpβ37, Tyrα42, Tyrα140, and Tyrβ145 at the α(1)-β(2) subunit interface underwent transitions between two contact states (named as T and R) upon ligand binding, while Trpα14, Trpβ15, and Tyrβ35 displayed little changes. The corresponding spectral changes were identified only for the α(2)β(2) tetramer, but not the isolated α and β chains in the oligomeric forms, and therefore were exclusively attributed to a quaternary structure change. Ligand binding as well as allosteric effectors and pH altered only the number of the T-contacted Tyr and Trp residues without varying the two contact states themselves. A new method to semiquantitatively evaluate the amount of T-contacted Tyr and Trp residues in a given liganded form is here proposed, and with it a quaternary structure was determined for various symmetrically half-liganded forms obtained with ligand-hybrid, metal-hybrid, and valency-hybrid Hbs. It was found that ligand binding to the α or β subunits yielded different subunit contacts and that the contact changes of the Trp and Tyr residues were not always concerted. The contact changes at the α(1)-β(2) (α(2)-β(1)) interface are correlated with the proximal strain exerted on the Fe-His(F8) bond, which is noted to be much larger in the α than β subunits in the α(2)β(2) tetramer." @default.
- W2335172489 created "2016-06-24" @default.
- W2335172489 creator A5016679774 @default.
- W2335172489 creator A5078089155 @default.
- W2335172489 creator A5088930598 @default.
- W2335172489 date "2011-06-09" @default.
- W2335172489 modified "2023-09-23" @default.
- W2335172489 title "A New Way To Understand Quaternary Structure Changes of Hemoglobin upon Ligand Binding On the Basis of UV-Resonance Raman Evaluation of Intersubunit Interactions" @default.
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- W2335172489 doi "https://doi.org/10.1021/ja111370f" @default.
- W2335172489 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21615086" @default.
- W2335172489 hasPublicationYear "2011" @default.
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