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

Kusai A. Merchant; W. G. Noid; David E. Thompson; Ryo Akiyama; Roger F. Loring; M. D. Fayer

doi:10.1021/jp026793o

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

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

Research output: Contribution to journal › Article › peer-review

80 Scopus citations

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 N_ε-H proton and N_δ of His64 are equidistant from the ligand, whereas in the A₃ substate, the N_ε-H of His64 is oriented toward the CO.

Original language	English (US)
Pages (from-to)	4-7
Number of pages	4
Journal	Journal of Physical Chemistry B
Volume	107
Issue number	1
DOIs	https://doi.org/10.1021/jp026793o
State	Published - Jan 9 2003

All Science Journal Classification (ASJC) codes

Physical and Theoretical Chemistry
Surfaces, Coatings and Films
Materials Chemistry

Access to Document

10.1021/jp026793o

Cite this

@article{f0bfa13aefc948fa9b9410ad7981cbdf,

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

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.",

author = "Merchant, {Kusai A.} and Noid, {W. G.} and Thompson, {David E.} and Ryo Akiyama and Loring, {Roger F.} and Fayer, {M. D.}",

year = "2003",

month = jan,

day = "9",

doi = "10.1021/jp026793o",

language = "English (US)",

volume = "107",

pages = "4--7",

journal = "Journal of Physical Chemistry B",

issn = "1089-5647",

number = "1",

}

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, W. G.

AU - Thompson, David E.

AU - Akiyama, Ryo

AU - Loring, Roger F.

AU - Fayer, M. D.

PY - 2003/1/9

Y1 - 2003/1/9

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=0037426830&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0037426830&partnerID=8YFLogxK

U2 - 10.1021/jp026793o

DO - 10.1021/jp026793o

M3 - Article

AN - SCOPUS:0037426830

SN - 1089-5647

VL - 107

SP - 4

EP - 7

JO - Journal of Physical Chemistry B

JF - Journal of Physical Chemistry B

IS - 1

ER -

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

Abstract

All Science Journal Classification (ASJC) codes

Access to Document

Other files and links

Fingerprint

Cite this