Structural assignments and dynamics of the a substates of MbCo: Spectrally resolved vibrational echo experiments and molecular dynamics simulations

Kusai A. Merchant, William George Noid, David E. Thompson, Ryo Akiyama, Roger F. Loring, M. D. Fayer

Research output: Contribution to journalArticle

73 Citations (Scopus)

Abstract

Spectrally resolved three-pulse stimulated vibrational echo experiments are used as the basis for structural assignments of the A1 and A3 spectroscopic substates in the IR spectrum of the carbon monoxide (CO) stretch of carbonmonoxymyoglobin (MbCO). The measured dephasing dynamics of these substates is compared to the dephasing dynamics of MbCO predicted from molecular dynamics (MD) simulations. We assign the A1 and A3 substates to different protein conformations on the basis of the agreement between the measured and computed vibrational echoes. In the A1 substate, the Nε-H proton and Nδ of His64 are equidistant from the ligand, whereas in the A3 substate, the Nε-H of His64 is oriented toward the CO.

Original languageEnglish (US)
Pages (from-to)4-7
Number of pages4
JournalJournal of Physical Chemistry B
Volume107
Issue number1
DOIs
StatePublished - Jan 9 2003

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Carbon Monoxide
carbon monoxide
Molecular dynamics
echoes
molecular dynamics
Computer simulation
Conformations
Protons
simulation
Experiments
Ligands
proteins
ligands
protons
pulses
Proteins
carboxymyoglobin

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Surfaces, Coatings and Films
  • Materials Chemistry

Cite this

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abstract = "Spectrally resolved three-pulse stimulated vibrational echo experiments are used as the basis for structural assignments of the A1 and A3 spectroscopic substates in the IR spectrum of the carbon monoxide (CO) stretch of carbonmonoxymyoglobin (MbCO). The measured dephasing dynamics of these substates is compared to the dephasing dynamics of MbCO predicted from molecular dynamics (MD) simulations. We assign the A1 and A3 substates to different protein conformations on the basis of the agreement between the measured and computed vibrational echoes. In the A1 substate, the Nε-H proton and Nδ of His64 are equidistant from the ligand, whereas in the A3 substate, the Nε-H of His64 is oriented toward the CO.",
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Structural assignments and dynamics of the a substates of MbCo : Spectrally resolved vibrational echo experiments and molecular dynamics simulations. / Merchant, Kusai A.; Noid, William George; Thompson, David E.; Akiyama, Ryo; Loring, Roger F.; Fayer, M. D.

In: Journal of Physical Chemistry B, Vol. 107, No. 1, 09.01.2003, p. 4-7.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Structural assignments and dynamics of the a substates of MbCo

T2 - Spectrally resolved vibrational echo experiments and molecular dynamics simulations

AU - Merchant, Kusai A.

AU - Noid, William George

AU - Thompson, David E.

AU - Akiyama, Ryo

AU - Loring, Roger F.

AU - Fayer, M. D.

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AB - Spectrally resolved three-pulse stimulated vibrational echo experiments are used as the basis for structural assignments of the A1 and A3 spectroscopic substates in the IR spectrum of the carbon monoxide (CO) stretch of carbonmonoxymyoglobin (MbCO). The measured dephasing dynamics of these substates is compared to the dephasing dynamics of MbCO predicted from molecular dynamics (MD) simulations. We assign the A1 and A3 substates to different protein conformations on the basis of the agreement between the measured and computed vibrational echoes. In the A1 substate, the Nε-H proton and Nδ of His64 are equidistant from the ligand, whereas in the A3 substate, the Nε-H of His64 is oriented toward the CO.

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