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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2004-9-3
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pubmed:abstractText |
The dynamics of the ferric CN complexes of the heme proteins Myoglobin and Hemoglobin I from the clam Lucina pectinata upon Soret band excitation is monitored using infrared and broad band visible pump-probe spectroscopy. The transient response in the UV-vis spectral region does not depend on the heme pocket environment and is very similar to that known for ferrous proteins. The main feature is an instantaneous, broad, short-lived absorption signal that develops into a narrower red-shifted Soret band. Significant transient absorption is also observed in the 360-390 nm range. At all probe wavelengths the signal decays to zero with a longest time constant of 3.6 ps. The infrared data on MbCN reveal a bleaching of the C triple bond N stretch vibration of the heme-bound ligand, and the formation of a five-times weaker transient absorption band, 28 cm(-1) lower in energy, within the time resolution of the experiment. The MbC triple bond N stretch vibration provides a direct measure for the return of population to the ligated electronic (and vibrational) ground state with a 3-4 ps time constant. In addition, the CN-stretch frequency is sensitive to the excitation of low frequency heme modes, and yields independent information about vibrational cooling, which occurs on the same timescale.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-10231545,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-10512835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-11325737,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-11341838,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-12010067,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-12773621,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-2398044,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-3393531,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-3415972,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-3427114,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-3972836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-7638619,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-7966324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-8519962,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-8611547,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-9109658,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-9334299,
http://linkedlifedata.com/resource/pubmed/commentcorrection/15345566-9510522
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-3495
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pubmed:author |
pubmed-author:BonacinaLuigiL,
pubmed-author:BredenbeckJensJ,
pubmed-author:ChaussardFrédéricF,
pubmed-author:CherguiMajedM,
pubmed-author:Gonzalez-GonzalezAlejandroA,
pubmed-author:HammPeterP,
pubmed-author:HelbingJanJ,
pubmed-author:López-GarrigaJuanJ,
pubmed-author:PietriRuthR,
pubmed-author:Ramos-AlvarezCacimarC,
pubmed-author:RuizCarlosC,
pubmed-author:van MourikFrankF
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pubmed:issnType |
Print
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pubmed:volume |
87
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1881-91
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:15345566-Animals,
pubmed-meshheading:15345566-Electrons,
pubmed-meshheading:15345566-Heme,
pubmed-meshheading:15345566-Hemoglobins,
pubmed-meshheading:15345566-Horses,
pubmed-meshheading:15345566-Iron,
pubmed-meshheading:15345566-Kinetics,
pubmed-meshheading:15345566-Lasers,
pubmed-meshheading:15345566-Mollusca,
pubmed-meshheading:15345566-Muscle, Skeletal,
pubmed-meshheading:15345566-Myoglobin,
pubmed-meshheading:15345566-Spectrophotometry,
pubmed-meshheading:15345566-Spectrophotometry, Infrared,
pubmed-meshheading:15345566-Spectroscopy, Fourier Transform Infrared,
pubmed-meshheading:15345566-Time Factors,
pubmed-meshheading:15345566-Ultraviolet Rays
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pubmed:year |
2004
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pubmed:articleTitle |
Time-resolved visible and infrared study of the cyano complexes of myoglobin and of hemoglobin I from Lucina pectinata.
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pubmed:affiliation |
Physikalisch-Chemisches Institut, Universität Zürich, 8057 Zürich, Switzerland. j.helbing@pci.unizh.ch
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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