Allosteric transitions in hemoglobin revisited

Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, ther...

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Published inBiochimica et biophysica acta. General subjects Vol. 1864; no. 2; p. 129335
Main Author Shibayama, Naoya
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.02.2020
Subjects
Allosteric regulation
Allostery
Conformational change
Hemoglobin
humans
ligands
oxygen
Protein function
structure-activity relationships
X-ray crystallography
XL[α(Fe)β(Ni)]2
HL
nmax
FL
Conformational change
PDB
X-ray crystallography
IHP
R
XL[α(Ni)β(Fe)]2
T
Protein function
Hemoglobin
Pi
R2
Allostery
RMSD
P50
BZF
XL[α(Fe-CO)β(Ni)][α(Ni)β(Fe-CO)]
XL[α(Fe)β(Ni)][α(Ni)β(Fe)]
RR2
PEG
Allosteric regulation
BPG
XL[α(Fe)β(Fe)][α(Ni)β(Ni)]
TR
Ki
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Abstract Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, there is renewed interest in this topic due to recent experimental breakthroughs that show how hemoglobin actually undergoes conformational transitions in response to environmental changes. I review the current understanding of hemoglobin structure-function relationships revealed by recent discoveries. A unique single crystal, in which three protein molecules are allowed to express a whole range of quaternary structures, helped to reveal the detailed transition pathway including various intermediate forms. I also discuss the potential of single-molecule techniques that are currently under examination. New crystallographic approaches reveal that the hemoglobin allosteric transition involves population shifts in multiple quaternary conformers rather than a simple two-state switch, and that coexisting individual conformers may have disproportionate effects on the apparent O2 affinity of hemoglobin. These approaches provide a further level of complexity on the textbook statement of hemoglobin allostery, highlighting the relevance of conformational distributions in controlling the function and regulation of allosteric proteins. •Despite much effort, structural basis for hemoglobin allostery has been controversial.•A unique single crystal can reveal the full allosteric pathway in hemoglobin.•Results clarify equilibria of multiple conformations including a third affinity state.•Conformational population shifts are critical to hemoglobin allostery.•Conformational population shifts are consistent with the concerted MWC model.
AbstractList Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, there is renewed interest in this topic due to recent experimental breakthroughs that show how hemoglobin actually undergoes conformational transitions in response to environmental changes.BACKGROUNDHuman hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, there is renewed interest in this topic due to recent experimental breakthroughs that show how hemoglobin actually undergoes conformational transitions in response to environmental changes.I review the current understanding of hemoglobin structure-function relationships revealed by recent discoveries. A unique single crystal, in which three protein molecules are allowed to express a whole range of quaternary structures, helped to reveal the detailed transition pathway including various intermediate forms. I also discuss the potential of single-molecule techniques that are currently under examination.SCOPE OF REVIEWI review the current understanding of hemoglobin structure-function relationships revealed by recent discoveries. A unique single crystal, in which three protein molecules are allowed to express a whole range of quaternary structures, helped to reveal the detailed transition pathway including various intermediate forms. I also discuss the potential of single-molecule techniques that are currently under examination.New crystallographic approaches reveal that the hemoglobin allosteric transition involves population shifts in multiple quaternary conformers rather than a simple two-state switch, and that coexisting individual conformers may have disproportionate effects on the apparent O2 affinity of hemoglobin.MAJOR CONCLUSIONSNew crystallographic approaches reveal that the hemoglobin allosteric transition involves population shifts in multiple quaternary conformers rather than a simple two-state switch, and that coexisting individual conformers may have disproportionate effects on the apparent O2 affinity of hemoglobin.These approaches provide a further level of complexity on the textbook statement of hemoglobin allostery, highlighting the relevance of conformational distributions in controlling the function and regulation of allosteric proteins.GENERAL SIGNIFICANCEThese approaches provide a further level of complexity on the textbook statement of hemoglobin allostery, highlighting the relevance of conformational distributions in controlling the function and regulation of allosteric proteins.
Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, there is renewed interest in this topic due to recent experimental breakthroughs that show how hemoglobin actually undergoes conformational transitions in response to environmental changes.I review the current understanding of hemoglobin structure-function relationships revealed by recent discoveries. A unique single crystal, in which three protein molecules are allowed to express a whole range of quaternary structures, helped to reveal the detailed transition pathway including various intermediate forms. I also discuss the potential of single-molecule techniques that are currently under examination.New crystallographic approaches reveal that the hemoglobin allosteric transition involves population shifts in multiple quaternary conformers rather than a simple two-state switch, and that coexisting individual conformers may have disproportionate effects on the apparent O₂ affinity of hemoglobin.These approaches provide a further level of complexity on the textbook statement of hemoglobin allostery, highlighting the relevance of conformational distributions in controlling the function and regulation of allosteric proteins.
Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, there is renewed interest in this topic due to recent experimental breakthroughs that show how hemoglobin actually undergoes conformational transitions in response to environmental changes. I review the current understanding of hemoglobin structure-function relationships revealed by recent discoveries. A unique single crystal, in which three protein molecules are allowed to express a whole range of quaternary structures, helped to reveal the detailed transition pathway including various intermediate forms. I also discuss the potential of single-molecule techniques that are currently under examination. New crystallographic approaches reveal that the hemoglobin allosteric transition involves population shifts in multiple quaternary conformers rather than a simple two-state switch, and that coexisting individual conformers may have disproportionate effects on the apparent O affinity of hemoglobin. These approaches provide a further level of complexity on the textbook statement of hemoglobin allostery, highlighting the relevance of conformational distributions in controlling the function and regulation of allosteric proteins.
Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model without intermediates offers a simple qualitative description of the allosteric behavior of hemoglobin, as presented in textbooks. However, there is renewed interest in this topic due to recent experimental breakthroughs that show how hemoglobin actually undergoes conformational transitions in response to environmental changes. I review the current understanding of hemoglobin structure-function relationships revealed by recent discoveries. A unique single crystal, in which three protein molecules are allowed to express a whole range of quaternary structures, helped to reveal the detailed transition pathway including various intermediate forms. I also discuss the potential of single-molecule techniques that are currently under examination. New crystallographic approaches reveal that the hemoglobin allosteric transition involves population shifts in multiple quaternary conformers rather than a simple two-state switch, and that coexisting individual conformers may have disproportionate effects on the apparent O2 affinity of hemoglobin. These approaches provide a further level of complexity on the textbook statement of hemoglobin allostery, highlighting the relevance of conformational distributions in controlling the function and regulation of allosteric proteins. •Despite much effort, structural basis for hemoglobin allostery has been controversial.•A unique single crystal can reveal the full allosteric pathway in hemoglobin.•Results clarify equilibria of multiple conformations including a third affinity state.•Conformational population shifts are critical to hemoglobin allostery.•Conformational population shifts are consistent with the concerted MWC model.
ArticleNumber 129335
Author Shibayama, Naoya
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  email: shibayam@jichi.ac.jp
  organization: Division of Biophysics, Department of Physiology, Jichi Medical University, 3311-1 Yakushiji, Shimotsuke, Tochigi 329-0498, Japan
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Keywords XL[α(Fe)β(Ni)]2
HL
nmax
FL
Conformational change
PDB
X-ray crystallography
IHP
R
XL[α(Ni)β(Fe)]2
T
Protein function
Hemoglobin
Pi
R2
Allostery
RMSD
P50
BZF
XL[α(Fe-CO)β(Ni)][α(Ni)β(Fe-CO)]
XL[α(Fe)β(Ni)][α(Ni)β(Fe)]
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Snippet Human hemoglobin is an allosteric protein that exerts exquisite control over ligand binding through large-scale conformational changes. The two-state model...
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SubjectTerms Allosteric regulation
Allostery
Conformational change
Hemoglobin
humans
ligands
oxygen
Protein function
structure-activity relationships
X-ray crystallography
Title Allosteric transitions in hemoglobin revisited
URI https://dx.doi.org/10.1016/j.bbagen.2019.03.021
https://www.ncbi.nlm.nih.gov/pubmed/30951803
https://www.proquest.com/docview/2204696143
https://www.proquest.com/docview/2253201101
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