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- W2044666108 abstract "Time-resolved circular dichroism (TRCD) studies performed on photolyzed hemoglobin−CO complex (HbCO) probe room temperature protein relaxations in Hb, including the R → T allosteric transition. TRCD spectroscopy of photolysis intermediates in the near-UV (250−400 nm) spectral region provides a diagnostic for T-like structure at the α1β2 interface via the effect of quaternary structure on the UV CD of aromatic residues. The TRCD of porphyrin-based transitions in the UV and Soret regions, reflecting transition-dipole couplings between hemes and aromatic residues over a radius wide enough to permit heme-interface and inter-dimer interactions, is modulated by the tertiary and quaternary structure of photolysis intermediates. In the allosteric core model of Hb cooperativity, Fe−CO bond breakage initiates a heme structural change, thought to be heme doming, that is transmitted to the α1β2 interface via the F helix. The TRCD results, analyzed in light of kinetic information from time-resolved absorption studies, suggest specific features for the mechanism by which the ensuing tertiary and quaternary conformational changes propagate through the protein. In particular, the UV-TRCD indicates that the α1β2 interface responds within several hundred nanoseconds to initial events at the heme by shifting from an R toward a T-like interface. The appearance of T-like character at the α1β2 interface tens of microseconds before the appearance of equilibrated T state deoxyHb indicates that the R → T transition in photolyzed HbCO is a stepwise process, as previously suggested by time-resolved resonance Raman studies." @default.
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- W2044666108 date "1996-01-01" @default.
- W2044666108 modified "2023-10-12" @default.
- W2044666108 title "Allosteric Intermediates in Hemoglobin. 1. Nanosecond Time-Resolved Circular Dichroism Spectroscopy" @default.
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- W2044666108 doi "https://doi.org/10.1021/bi952247s" @default.
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