ArticleJournal of the American Chemical Society2012
Heme reactivity is uncoupled from quaternary structure in gel-encapsulated hemoglobin: a resonance Raman spectroscopic study.
Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Analysis of β-C-terminal salt bridges in T-state hemoglobin by trapping tertiary conformations in silica gels.Protein science : a publication of the Protein Society · 2025Article
- Structural origin of cooperativity in human hemoglobin: a view from different roles of α and β subunits in the αBiophysical reviews · 2022Review
- Haemoglobin(βK120C)-albumin trimer as an artificial ORSC chemical biology · 2020Article
- Modulation of hemoglobin dynamics by an allosteric effector.Protein science : a publication of the Protein Society · 2017Article
- 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
- Differential control of heme reactivity in alpha and beta subunits of hemoglobin: a combined Raman spectroscopic and computational study.Journal of the American Chemical Society · 2014Article
- Mapping polymerization and allostery of hemoglobin S using point mutations.The journal of physical chemistry. B · 2013Article
- Tertiary and quaternary allostery in tetrameric hemoglobin from Scapharca inaequivalvis.Biochemistry · 2013Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Encapsulation of hemoglobin (Hb) in silica gel preserves structure and function but greatly slows protein motion, thereby providing access to intermediates along the allosteric pathway that are inaccessible in solution. Resonance Raman (RR) spectroscopy with visible and ultraviolet laser excitation provides probes of heme reactivity and of key tertiary and quaternary contacts. These probes were monitored in gels after deoxygenation of oxyHb and after CO binding to deoxyHb, which initiate conformational change in the R-T and T-R directions, respectively. The spectra establish that quaternary structure change in the gel takes a week or more but that the evolution of heme reactivity, as monitored by the Fe-histidine stretching vibration, ν(FeHis), is completed within two days, and is therefore uncoupled from the quaternary structure. Within each quaternary structure, the evolving ν(FeHis) frequencies span the full range of values between those previously associated with the high- and low-affinity end states, R and T. This result supports the tertiary two-state (TTS) model, in which the Hb subunits can adopt high- and low-affinity tertiary structures, r and t, within each quaternary state. The spectra also reveal different tertiary pathways, involving the breaking and reformation of E and F interhelical contacts in the R-T direction but not the T-R direction. In the latter, tertiary motions are restricted by the T quaternary contacts.
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