Picosecond Structural Dynamics of Myoglobin following Photolysis of Carbon Monoxide
We have used picosecond infrared (IR) transient absorption spectroscopy in the amide I band to probe the dynamics of protein motion of myoglobin (Mb) following the photolysis of carbon monoxide. The rise time of the deoxy protein conformation is shown to be about 8 ps. The spectrum of amide I change...
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| Veröffentlicht in: | Journal of Physical Chemistry 1996-02, Vol.100 (8), p.3273-3277 |
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| container_title | Journal of Physical Chemistry |
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| creator | Causgrove, Timothy P Dyer, R. Brian |
| description | We have used picosecond infrared (IR) transient absorption spectroscopy in the amide I band to probe the dynamics of protein motion of myoglobin (Mb) following the photolysis of carbon monoxide. The rise time of the deoxy protein conformation is shown to be about 8 ps. The spectrum of amide I changes was also measured at 50 ps after photolysis and found to be similar to static IR difference spectra and to time-resolved IR spectra taken at times longer than 100 ns. By comparing the results obtained here with other picosecond results on photolysis of CO from Mb, we conclude that the majority of changes seen in the amide I spectra are due to global motion on the proximal side of the heme. The time scale for amide I changes are compared to the results of molecular dynamics calculations. |
| doi_str_mv | 10.1021/jp952483c |
| format | Article |
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Brian</creator><creatorcontrib>Causgrove, Timothy P ; Dyer, R. Brian</creatorcontrib><description>We have used picosecond infrared (IR) transient absorption spectroscopy in the amide I band to probe the dynamics of protein motion of myoglobin (Mb) following the photolysis of carbon monoxide. The rise time of the deoxy protein conformation is shown to be about 8 ps. The spectrum of amide I changes was also measured at 50 ps after photolysis and found to be similar to static IR difference spectra and to time-resolved IR spectra taken at times longer than 100 ns. By comparing the results obtained here with other picosecond results on photolysis of CO from Mb, we conclude that the majority of changes seen in the amide I spectra are due to global motion on the proximal side of the heme. 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Brian</creatorcontrib><title>Picosecond Structural Dynamics of Myoglobin following Photolysis of Carbon Monoxide</title><title>Journal of Physical Chemistry</title><addtitle>J. Phys. Chem</addtitle><description>We have used picosecond infrared (IR) transient absorption spectroscopy in the amide I band to probe the dynamics of protein motion of myoglobin (Mb) following the photolysis of carbon monoxide. The rise time of the deoxy protein conformation is shown to be about 8 ps. The spectrum of amide I changes was also measured at 50 ps after photolysis and found to be similar to static IR difference spectra and to time-resolved IR spectra taken at times longer than 100 ns. By comparing the results obtained here with other picosecond results on photolysis of CO from Mb, we conclude that the majority of changes seen in the amide I spectra are due to global motion on the proximal side of the heme. The time scale for amide I changes are compared to the results of molecular dynamics calculations.</description><subject>40 CHEMISTRY</subject><subject>ABSORPTION SPECTRA</subject><subject>BIOLOGY AND MEDICINE, BASIC STUDIES</subject><subject>CARBON MONOXIDE</subject><subject>DYNAMICS</subject><subject>MOLECULAR STRUCTURE</subject><subject>MYOGLOBIN</subject><subject>PHOTOLYSIS</subject><subject>STRUCTURAL CHEMICAL ANALYSIS</subject><issn>0022-3654</issn><issn>1541-5740</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><recordid>eNpt0DtPwzAUBWALgUQpDPyDMDAwBPyI43aE8lYrKrUsLJbt2K1Lale2K5p_TyCoE9OVrj4d6RwAzhG8RhCjm9VmSHExIOoA9BAtUE5ZAQ9BD0KMc1LS4hicxLiCECJCUA_Mplb5qJV3VTZLYavSNog6u2-cWFsVM2-ySeMXtZfWZcbXtf-ybpFNlz75uon2V4xEkN5lE-_8zlb6FBwZUUd99nf74P3xYT56zsdvTy-j23EuyICl3MCioFoLglnFGMJlYUoojaSSCaiNFO2DDaVCpVC4opVkpJJDjbFShlZYkD646HJ9TJZHZZNWy7aJ0ypxjIYM4tZcdUYFH2PQhm-CXYvQcAT5z2J8v1hr887amPRuD0X45CUjjPL5dMYx-Xil5V3J562_7LxQka_8Nri27T-53_Zdev0</recordid><startdate>19960222</startdate><enddate>19960222</enddate><creator>Causgrove, Timothy P</creator><creator>Dyer, R. 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Brian</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a387t-f0445eea327d771264f60bfb5b7a0efba64f79bc16ac2d5db73db9e22ccf5d2a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>40 CHEMISTRY</topic><topic>ABSORPTION SPECTRA</topic><topic>BIOLOGY AND MEDICINE, BASIC STUDIES</topic><topic>CARBON MONOXIDE</topic><topic>DYNAMICS</topic><topic>MOLECULAR STRUCTURE</topic><topic>MYOGLOBIN</topic><topic>PHOTOLYSIS</topic><topic>STRUCTURAL CHEMICAL ANALYSIS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Causgrove, Timothy P</creatorcontrib><creatorcontrib>Dyer, R. Brian</creatorcontrib><collection>Istex</collection><collection>CrossRef</collection><collection>OSTI.GOV</collection><jtitle>Journal of Physical Chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Causgrove, Timothy P</au><au>Dyer, R. Brian</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Picosecond Structural Dynamics of Myoglobin following Photolysis of Carbon Monoxide</atitle><jtitle>Journal of Physical Chemistry</jtitle><addtitle>J. Phys. Chem</addtitle><date>1996-02-22</date><risdate>1996</risdate><volume>100</volume><issue>8</issue><spage>3273</spage><epage>3277</epage><pages>3273-3277</pages><issn>0022-3654</issn><eissn>1541-5740</eissn><abstract>We have used picosecond infrared (IR) transient absorption spectroscopy in the amide I band to probe the dynamics of protein motion of myoglobin (Mb) following the photolysis of carbon monoxide. The rise time of the deoxy protein conformation is shown to be about 8 ps. The spectrum of amide I changes was also measured at 50 ps after photolysis and found to be similar to static IR difference spectra and to time-resolved IR spectra taken at times longer than 100 ns. By comparing the results obtained here with other picosecond results on photolysis of CO from Mb, we conclude that the majority of changes seen in the amide I spectra are due to global motion on the proximal side of the heme. The time scale for amide I changes are compared to the results of molecular dynamics calculations.</abstract><cop>United States</cop><pub>American Chemical Society</pub><doi>10.1021/jp952483c</doi><tpages>5</tpages></addata></record> |
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| ispartof | Journal of Physical Chemistry, 1996-02, Vol.100 (8), p.3273-3277 |
| issn | 0022-3654 1541-5740 |
| language | eng |
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| source | ACS Publications |
| subjects | 40 CHEMISTRY ABSORPTION SPECTRA BIOLOGY AND MEDICINE, BASIC STUDIES CARBON MONOXIDE DYNAMICS MOLECULAR STRUCTURE MYOGLOBIN PHOTOLYSIS STRUCTURAL CHEMICAL ANALYSIS |
| title | Picosecond Structural Dynamics of Myoglobin following Photolysis of Carbon Monoxide |
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