2006
DOI: 10.1021/bi061451k
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An Optical Signal Correlated with the Allosteric Transition in Scapharca inaequivalvis HbI

Abstract: The transient absorbance change in the first 2 μs after photolysis of COHbI (from Scapharca inaequivalvis) reported by Chiancone et al.(1) has been studied in several mutants. Evidence is presented that this change (rts) is associated with the allosteric transition between R-and T-states. Two different rts spectra relate to Hb 2 and Hb 2 CO. No rts has been observed for mutants at position 97 (normally Phe). Correlation of ligand binding and rts shows that protein function changes at or near the rates of rts -… Show more

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Cited by 9 publications
(18 citation statements)
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“…The bimolecular recombination of I 3 of F97Y HbI (1300 mM −1 s −1 ) is accelerated by almost thirteen times compared with that of WT HbI (95 mM −1 s −1 ). The acceleration of the bimolecular recombination of F97Y HbI is consistent with the results of flash photolysis and equilibrium oxygen binding experiments [ 9 , 13 , 17 , 20 , 22 ].…”
Section: Structural Dynamics Of Hbi Studied By Trxsssupporting
confidence: 87%
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“…The bimolecular recombination of I 3 of F97Y HbI (1300 mM −1 s −1 ) is accelerated by almost thirteen times compared with that of WT HbI (95 mM −1 s −1 ). The acceleration of the bimolecular recombination of F97Y HbI is consistent with the results of flash photolysis and equilibrium oxygen binding experiments [ 9 , 13 , 17 , 20 , 22 ].…”
Section: Structural Dynamics Of Hbi Studied By Trxsssupporting
confidence: 87%
“…However, the allosteric structural transition of Hb is still elusive because of the complex kinetics arising from its heteromeric tetramer structure. In this respect, homodimeric hemoglobin (HbI) from Scapharca inaequivalvis has served as an excellent model system for investigating the allosteric structural transition between a ligated R state with high ligand affinity and a deoxygenated T state with low ligand affinity [ 8 , 9 , 10 , 11 , 12 , 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 , 22 , 23 , 24 , 25 , 26 , 27 , 28 , 29 , 30 , 31 , 32 , 33 , 34 , 35 , 36 , 37 , 38 ] due to its simpler dimeric structure. In the HbI, the E and F helices of monomers are located at the interface of homodimer [ 11 , 12 , 39 ], which is often referred to as EF dimer.…”
Section: Introductionmentioning
confidence: 99%
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“…The first passage time was estimated as 10 6 9 ms. Although the error bars are large, the results are within experimental values (14,15).…”
supporting
confidence: 77%