Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations
The vibrational energy relaxation of carbon monoxide in the heme pocket of sperm whale myoglobin was studied by using molecular dynamics simulation and normal mode analysis methods. Molecular dynamics trajectories of solvated myoglobin were run at 300 K for both the δ- and ɛ-tautomers of the distal...
Main Authors: | , , , , |
---|---|
Format: | Text |
Language: | English |
Published: |
The National Academy of Sciences
1999
|
Subjects: | |
Online Access: | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC24435 http://www.ncbi.nlm.nih.gov/pubmed/10588704 |
id |
ftpubmed:oai:pubmedcentral.nih.gov:24435 |
---|---|
record_format |
openpolar |
spelling |
ftpubmed:oai:pubmedcentral.nih.gov:24435 2023-05-15T18:26:47+02:00 Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations Sagnella, Diane E. Straub, John E. Jackson, Timothy A. Lim, Manho Anfinrud, Philip A. 1999-12-07 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC24435 http://www.ncbi.nlm.nih.gov/pubmed/10588704 en eng The National Academy of Sciences http://www.ncbi.nlm.nih.gov/pmc/articles/PMC24435 http://www.ncbi.nlm.nih.gov/pubmed/10588704 Copyright © 1999, The National Academy of Sciences Biological Sciences Text 1999 ftpubmed 2013-08-29T07:12:31Z The vibrational energy relaxation of carbon monoxide in the heme pocket of sperm whale myoglobin was studied by using molecular dynamics simulation and normal mode analysis methods. Molecular dynamics trajectories of solvated myoglobin were run at 300 K for both the δ- and ɛ-tautomers of the distal His-64. Vibrational population relaxation times of 335 ± 115 ps for the δ-tautomer and 640 ± 185 ps for the ɛ-tautomer were estimated by using the Landau–Teller model. Normal mode analysis was used to identify those protein residues that act as the primary “doorway” modes in the vibrational relaxation of the oscillator. Although the CO relaxation rates in both the ɛ- and δ-tautomers are similar in magnitude, the simulations predict that the vibrational relaxation of the CO is faster in the δ-tautomer with the distal His playing an important role in the energy relaxation mechanism. Time-resolved mid-IR absorbance measurements were performed on photolyzed carbonmonoxy hemoglobin (Hb13CO). From these measurements, a T1 time of 600 ± 150 ps was determined. The simulation and experimental estimates are compared and discussed. Text Sperm whale PubMed Central (PMC) |
institution |
Open Polar |
collection |
PubMed Central (PMC) |
op_collection_id |
ftpubmed |
language |
English |
topic |
Biological Sciences |
spellingShingle |
Biological Sciences Sagnella, Diane E. Straub, John E. Jackson, Timothy A. Lim, Manho Anfinrud, Philip A. Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations |
topic_facet |
Biological Sciences |
description |
The vibrational energy relaxation of carbon monoxide in the heme pocket of sperm whale myoglobin was studied by using molecular dynamics simulation and normal mode analysis methods. Molecular dynamics trajectories of solvated myoglobin were run at 300 K for both the δ- and ɛ-tautomers of the distal His-64. Vibrational population relaxation times of 335 ± 115 ps for the δ-tautomer and 640 ± 185 ps for the ɛ-tautomer were estimated by using the Landau–Teller model. Normal mode analysis was used to identify those protein residues that act as the primary “doorway” modes in the vibrational relaxation of the oscillator. Although the CO relaxation rates in both the ɛ- and δ-tautomers are similar in magnitude, the simulations predict that the vibrational relaxation of the CO is faster in the δ-tautomer with the distal His playing an important role in the energy relaxation mechanism. Time-resolved mid-IR absorbance measurements were performed on photolyzed carbonmonoxy hemoglobin (Hb13CO). From these measurements, a T1 time of 600 ± 150 ps was determined. The simulation and experimental estimates are compared and discussed. |
format |
Text |
author |
Sagnella, Diane E. Straub, John E. Jackson, Timothy A. Lim, Manho Anfinrud, Philip A. |
author_facet |
Sagnella, Diane E. Straub, John E. Jackson, Timothy A. Lim, Manho Anfinrud, Philip A. |
author_sort |
Sagnella, Diane E. |
title |
Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations |
title_short |
Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations |
title_full |
Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations |
title_fullStr |
Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations |
title_full_unstemmed |
Vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: Comparison of time-resolved mid-IR absorbance experiments and molecular dynamics simulations |
title_sort |
vibrational population relaxation of carbon monoxide in the heme pocket of photolyzed carbonmonoxy myoglobin: comparison of time-resolved mid-ir absorbance experiments and molecular dynamics simulations |
publisher |
The National Academy of Sciences |
publishDate |
1999 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC24435 http://www.ncbi.nlm.nih.gov/pubmed/10588704 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC24435 http://www.ncbi.nlm.nih.gov/pubmed/10588704 |
op_rights |
Copyright © 1999, The National Academy of Sciences |
_version_ |
1766208748671467520 |