The apolar distal histidine mutant (His69 → Val) of the homodimeric Scapharca hemoglobin is in an R-like conformation

Laura Guarrera, Gianni Colotti, Alberto Boffi, Emilia Chiancone, Tapan Kanti Das, Denis L. Rousseau, Quentin H. Gibson

Research output: Contribution to journalArticle

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Abstract

The effect of the apolar mutation of the distal histidine (His69 → Val) has been studied in the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis. Absorption, circular dichroism, and resonance Raman spectroscopy point to a more symmetric heme structure of the deoxy derivative, which is indicative of an R-like conformation of the deoxy heme. Resonance Raman spectroscopy also brings out alterations in the geometry and interactions of the bound CO molecule. The iron-carbon stretching frequency is decreased by about 30 cm-1 with respect to the native protein, while the diatomic ligand stretching frequency is increased by about the same degree. Consistent with the structural changes, the ligand binding properties are significantly altered. In the mutant the overall rate and the affinity for CO binding are increased about 100-fold with respect to the native protein, and cooperativity is abolished. In addition, the amplitude and the rate of the geminate rebinding process increase significantly. This finding may be correlated to the longer average residence time of the photolyzed CO molecule within the heme pocket of the H69V mutant, as indicated by molecular dynamics simulations.

Original languageEnglish (US)
Pages (from-to)5608-5615
Number of pages8
JournalBiochemistry
Volume37
Issue number16
DOIs
StatePublished - Apr 21 1998

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Scapharca
Carbon Monoxide
Heme
Histidine
Conformations
Hemoglobins
Raman Spectrum Analysis
Stretching
Raman spectroscopy
Molluscs
Ligands
Molecules
Mollusca
Molecular Dynamics Simulation
Circular Dichroism
Molecular dynamics
Proteins
Carbon
Iron
Derivatives

ASJC Scopus subject areas

  • Biochemistry

Cite this

The apolar distal histidine mutant (His69 → Val) of the homodimeric Scapharca hemoglobin is in an R-like conformation. / Guarrera, Laura; Colotti, Gianni; Boffi, Alberto; Chiancone, Emilia; Das, Tapan Kanti; Rousseau, Denis L.; Gibson, Quentin H.

In: Biochemistry, Vol. 37, No. 16, 21.04.1998, p. 5608-5615.

Research output: Contribution to journalArticle

Guarrera, Laura ; Colotti, Gianni ; Boffi, Alberto ; Chiancone, Emilia ; Das, Tapan Kanti ; Rousseau, Denis L. ; Gibson, Quentin H. / The apolar distal histidine mutant (His69 → Val) of the homodimeric Scapharca hemoglobin is in an R-like conformation. In: Biochemistry. 1998 ; Vol. 37, No. 16. pp. 5608-5615.
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AU - Chiancone, Emilia

AU - Das, Tapan Kanti

AU - Rousseau, Denis L.

AU - Gibson, Quentin H.

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N2 - The effect of the apolar mutation of the distal histidine (His69 → Val) has been studied in the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis. Absorption, circular dichroism, and resonance Raman spectroscopy point to a more symmetric heme structure of the deoxy derivative, which is indicative of an R-like conformation of the deoxy heme. Resonance Raman spectroscopy also brings out alterations in the geometry and interactions of the bound CO molecule. The iron-carbon stretching frequency is decreased by about 30 cm-1 with respect to the native protein, while the diatomic ligand stretching frequency is increased by about the same degree. Consistent with the structural changes, the ligand binding properties are significantly altered. In the mutant the overall rate and the affinity for CO binding are increased about 100-fold with respect to the native protein, and cooperativity is abolished. In addition, the amplitude and the rate of the geminate rebinding process increase significantly. This finding may be correlated to the longer average residence time of the photolyzed CO molecule within the heme pocket of the H69V mutant, as indicated by molecular dynamics simulations.

AB - The effect of the apolar mutation of the distal histidine (His69 → Val) has been studied in the cooperative homodimeric hemoglobin from the mollusc Scapharca inaequivalvis. Absorption, circular dichroism, and resonance Raman spectroscopy point to a more symmetric heme structure of the deoxy derivative, which is indicative of an R-like conformation of the deoxy heme. Resonance Raman spectroscopy also brings out alterations in the geometry and interactions of the bound CO molecule. The iron-carbon stretching frequency is decreased by about 30 cm-1 with respect to the native protein, while the diatomic ligand stretching frequency is increased by about the same degree. Consistent with the structural changes, the ligand binding properties are significantly altered. In the mutant the overall rate and the affinity for CO binding are increased about 100-fold with respect to the native protein, and cooperativity is abolished. In addition, the amplitude and the rate of the geminate rebinding process increase significantly. This finding may be correlated to the longer average residence time of the photolyzed CO molecule within the heme pocket of the H69V mutant, as indicated by molecular dynamics simulations.

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