Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations
Spectrally resolved infrared stimulated vibrational echo data were obtained for sperm whale carbonmonoxymyoglobin (MbCO) at 300 K. The measured dephasing dynamics of the CO ligand are in agreement with dephasing dynamics calculated with molecular dynamics (MD) simulations for MbCO with the residue h...
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ftpubmed:oai:pubmedcentral.nih.gov:2435512 2023-05-15T18:26:47+02:00 Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations Merchant, Kusai A. Noid, W. G. Akiyama, Ryo Finkelstein, Ilya J. Goun, Alexei McClain, Brian L. Loring, Roger F. Fayer, M. D. 2003-11-12 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2435512 http://www.ncbi.nlm.nih.gov/pubmed/14599220 https://doi.org/10.1021/ja035654x en eng http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2435512 http://www.ncbi.nlm.nih.gov/pubmed/14599220 http://dx.doi.org/10.1021/ja035654x Article Text 2003 ftpubmed https://doi.org/10.1021/ja035654x 2013-09-02T00:43:26Z Spectrally resolved infrared stimulated vibrational echo data were obtained for sperm whale carbonmonoxymyoglobin (MbCO) at 300 K. The measured dephasing dynamics of the CO ligand are in agreement with dephasing dynamics calculated with molecular dynamics (MD) simulations for MbCO with the residue histidine-64 (His64) having its imidazole ε nitrogen protonated (Nε–H). The two conformational substate structures Bε and Rε observed in the MD simulations are assigned to the spectroscopic A1 and A3 conformational substates of MbCO, respectively, based on the agreement between the experimentally measured and calculated dephasing dynamics for these substates. In the A1 substate, the Nε–H proton and Nδ of His64 are approximately equidistant from the CO ligand, while in the A3 substate, the Nε–H of His64 is oriented toward the CO, and the Nδ is on the surface of the protein. The MD simulations show that dynamics of His64 represent the major source of vibrational dephasing of the CO ligand in the A3 state on both femtosecond and picosecond time scales. Dephasing in the A1 state is controlled by His64 on femtosecond time scales, and by the rest of the protein and the water solvent on longer time scales. Text Sperm whale PubMed Central (PMC) Journal of the American Chemical Society 125 45 13804 13818 |
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Article Merchant, Kusai A. Noid, W. G. Akiyama, Ryo Finkelstein, Ilya J. Goun, Alexei McClain, Brian L. Loring, Roger F. Fayer, M. D. Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations |
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Spectrally resolved infrared stimulated vibrational echo data were obtained for sperm whale carbonmonoxymyoglobin (MbCO) at 300 K. The measured dephasing dynamics of the CO ligand are in agreement with dephasing dynamics calculated with molecular dynamics (MD) simulations for MbCO with the residue histidine-64 (His64) having its imidazole ε nitrogen protonated (Nε–H). The two conformational substate structures Bε and Rε observed in the MD simulations are assigned to the spectroscopic A1 and A3 conformational substates of MbCO, respectively, based on the agreement between the experimentally measured and calculated dephasing dynamics for these substates. In the A1 substate, the Nε–H proton and Nδ of His64 are approximately equidistant from the CO ligand, while in the A3 substate, the Nε–H of His64 is oriented toward the CO, and the Nδ is on the surface of the protein. The MD simulations show that dynamics of His64 represent the major source of vibrational dephasing of the CO ligand in the A3 state on both femtosecond and picosecond time scales. Dephasing in the A1 state is controlled by His64 on femtosecond time scales, and by the rest of the protein and the water solvent on longer time scales. |
format |
Text |
author |
Merchant, Kusai A. Noid, W. G. Akiyama, Ryo Finkelstein, Ilya J. Goun, Alexei McClain, Brian L. Loring, Roger F. Fayer, M. D. |
author_facet |
Merchant, Kusai A. Noid, W. G. Akiyama, Ryo Finkelstein, Ilya J. Goun, Alexei McClain, Brian L. Loring, Roger F. Fayer, M. D. |
author_sort |
Merchant, Kusai A. |
title |
Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations |
title_short |
Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations |
title_full |
Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations |
title_fullStr |
Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations |
title_full_unstemmed |
Myoglobin-CO Substate Structures and Dynamics: Multidimensional Vibrational Echoes and Molecular Dynamics Simulations |
title_sort |
myoglobin-co substate structures and dynamics: multidimensional vibrational echoes and molecular dynamics simulations |
publishDate |
2003 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2435512 http://www.ncbi.nlm.nih.gov/pubmed/14599220 https://doi.org/10.1021/ja035654x |
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Sperm whale |
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Sperm whale |
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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2435512 http://www.ncbi.nlm.nih.gov/pubmed/14599220 http://dx.doi.org/10.1021/ja035654x |
op_doi |
https://doi.org/10.1021/ja035654x |
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Journal of the American Chemical Society |
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125 |
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45 |
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13804 |
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13818 |
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1766208747661688832 |