ArticleJournal of the American Chemical Society2014
Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Direct observation of two-channel photodissociation of carbon monoxide from the hemoglobin subunits.Nature communications · 2025Article
- A retrospective on statistical mechanical models for hemoglobin allostery.The Journal of chemical physics · 2022Article
- Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the αBiophysical reviews · 2022Review
- Impact of hemoglobin biophysical studies on molecular pathogenesis and drug therapy for sickle cell disease.Molecular aspects of medicine · 2022Review
- Towards understanding non-equivalence of α and β subunits within human hemoglobin in conformational relaxation and molecular oxygen rebinding.Chemical science · 2021Article
- Haemoglobin(βK120C)-albumin trimer as an artificial ORSC chemical biology · 2020Article
- Kinetics of cyanide and carbon monoxide dissociation from ferrous human haptoglobin:hemoglobin(II) complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020Article
- Valid molecular dynamics simulations of human hemoglobin require a surprisingly large box size.eLife · 2018Article
- A role of heme side-chains of human hemoglobin in its function revealed by circular dichroism and resonance Raman spectroscopy.Biophysical reviews · 2018Review
- Article
- Tertiary and quaternary structural basis of oxygen affinity in human hemoglobin as revealed by multiscale simulations.Scientific reports · 2017Article
- Modulation of hemoglobin dynamics by an allosteric effector.Protein science : a publication of the Protein Society · 2017Article
- Role of Heme Pocket Water in Allosteric Regulation of Ligand Reactivity in Human Hemoglobin.Biochemistry · 2016Article
- Experiments on Hemoglobin in Single Crystals and Silica Gels Distinguish among Allosteric Models.Biophysical journal · 2015Article
- New look at hemoglobin allostery.Chemical reviews · 2015Review
- An Origin of Cooperative Oxygen Binding of Human Adult Hemoglobin: Different Roles of the α and β Subunits in the α2β2 Tetramer.PloS one · 2015Article
- From protein structure to function via single crystal optical spectroscopy.Frontiers in molecular biosciences · 2015Review
- Experimental basis for a new allosteric model for multisubunit proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
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9 authors.
Funding
Abstract
The use of hybrid hemoglobin (Hb), with mesoheme substituted for protoheme, allows separate monitoring of the α or β hemes along the allosteric pathway. Using resonance Raman (rR) spectroscopy in silica gel, which greatly slows protein motions, we have observed that the Fe-histidine stretching frequency, νFeHis, which is a monitor of heme reactivity, evolves between frequencies characteristic of the R and T states, for both α or β chains, prior to the quaternary R-T and T-R shifts. Computation of νFeHis, using QM/MM and the conformational search program PELE, produced remarkable agreement with experiment. Analysis of the PELE structures showed that the νFeHis shifts resulted from heme distortion and, in the α chain, Fe-His bond tilting. These results support the tertiary two-state model of ligand binding (Henry et al., Biophys. Chem. 2002, 98, 149). Experimentally, the νFeHis evolution is faster for β than for α chains, and pump-probe rR spectroscopy in solution reveals an inflection in the νFeHis time course at 3 μs for β but not for α hemes, an interval previously shown to be the first step in the R-T transition. In the α chain νFeHis dropped sharply at 20 μs, the final step in the R-T transition. The time courses are fully consistent with recent computational mapping of the R-T transition via conjugate peak refinement by Karplus and co-workers (Fischer et al., Proc. Natl. Acad. Sci. U. S. A. 2011, 108, 5608). The effector molecule IHP was found to lower νFeHis selectively for α chains within the R state, and a binding site in the α1α2 cleft is suggested.
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