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- W2034267975 abstract "The Fe-histidine stretching (nu(Fe-His)) frequency was determined for deoxy subunits of intermediately ligated human hemoglobin A in equilibrium and CO-photodissociated picosecond transient species in the presence and absence of strong allosteric effectors like inositol(hexakis)phosphate, bezafibrate, and 2,3-bisphosphoglycerate. The nu(Fe-His) frequency of deoxyHb A was unaltered by the effectors. The T-to-R transition occurred around m = 2-3 in the absence of effectors but m > 3.5 in their presence, where m is the average number of ligands bound to Hb and was determined from the intensity of the nu(4) band measured in the same experiment. The alpha1-beta2 subunit contacts revealed by ultraviolet resonance Raman spectra, which were distinctly different between the T and R states, remained unchanged by the effectors. This observation would solve the recent discrepancy that the strong effectors remove the cooperativity of oxygen binding in the low-affinity limit, whereas the (1)H NMR spectrum of fully ligated form exhibits the pattern of the R state." @default.
- W2034267975 created "2016-06-24" @default.
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- W2034267975 date "2005-08-01" @default.
- W2034267975 modified "2023-10-17" @default.
- W2034267975 title "Quaternary Structures of Intermediately Ligated Human Hemoglobin A and Influences from Strong Allosteric Effectors: Resonance Raman Investigation" @default.
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- W2034267975 doi "https://doi.org/10.1529/biophysj.104.049775" @default.
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