Conformational and functional significance of the α140 side-chain in HbA:: a UV and visible resonance Raman study of three α140 mutants
Conformational and functional significance of the α140 side-chain in HbA:: a UV and visible resonance Raman study of three α140 mutants
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DOI:
10.1002/jrs.1322
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发表时间:
2005-04-01
影响因子:
2.5
通讯作者:
Friedman, JM
中科院分区:
文献类型:
--
作者:
Juszczak, L;Samuni, U;Friedman, JM
Continuous wave UV resonance Raman (UVRR) and nanosecond time-resolved visible resonance Raman spectra were generated from the deoxy and CO derivatives of three alpha-chain mutants of human adult hemoglobin (HbA): Y alpha 140F, Y alpha 140G and Y alpha 140A. The UVRR results show that an aromatic side-chain in the alpha 140 site is needed for achieving the wild-type tertiary conformation in the allosterically important alpha(1)beta(2) interface for both the deoxy T state and the liganded R state. The wavenumbers of v(Fe-His), the iron-proximal histidine stretching mode, seen in the VRR spectra from the deoxy derivatives show that the hydrogen bond between alpha 140 tyrosine and the carbonyl of alpha 93 valine is necessary to obtain the full quaternary constraint associated with the deoxy T state even when the alpha(1)beta(2) interface is seemingly intact. A model is presented that describes the relationship between the packing of a cluster of residues linked to both W beta 37 and Y alpha 140 and the extent of proximal strain/quaternary constraint at the a-chain heme. The visible resonance Raman (VRR) spectra of the 8 ns photoproduct of the CO derivatives of the three mutants in the presence and absence of allosteric effectors show that all three mutants can access the R state but they show enhanced sensitivity to added IHP. The CO derivative of the Hb(Y alpha 140F) mutant in the presence of IHP exhibits properties consistent with the high-affinity T state observed both for non-equilibrium populations of HbA isolated using sol-gel matrices and for beta 37 mutants where the hinge region of the alpha(1)beta(2) interface is disrupted. Copyright (c) 2005 John Wiley & Sons, Ltd.