OSA's Digital Library

Applied Spectroscopy

Applied Spectroscopy

| PUBLISHED BY SAS — AVAILABLE FROM SAS AND OSA

  • Vol. 49, Iss. 6 — Jun. 1, 1995
  • pp: 702–708

Time-Resolved Step-Scan FT-IR Spectroscopy of the Photodynamics of Carbonmonoxymyoglobin

Susan E. Plunkett, James L. Chao, Thomas J. Tague, and Richard A. Palmer

Applied Spectroscopy, Vol. 49, Issue 6, pp. 702-708 (1995)


View Full Text Article

Acrobat PDF (702 KB)





Browse Journals / Lookup Meetings

Browse by Journal and Year


   


Lookup Conference Papers

Close Browse Journals / Lookup Meetings

Article Tools

Share
Citations
  • Export Citation/Save Click for help

Abstract

The kinetics of protein response and of CO recombination after photolysis of the Fe-CO bond in carbonmonoxymyoglobin have been monitored via time-resolved step-scan FT-IR absorption difference spectroscopy in D2O solution. Although the initial photodissociation is too fast to observe with currently available FT-IR instrumentation, we have been able to correlate the CO recombination kinetics with protein secondary structural changes via changes in the amide I band of the polypeptide chain with microsecond time resolution. The spectral and kinetic data corroborate and confirm previously published single-frequency infrared studies. This is the first application of time-resolved step-scan FT-IR spectroscopy in the absorbance difference mode to study the photodynamics of an aqueous protein solution at room temperature. This work also demonstrates the potential of the technique for the sub-microsecond kinetic analysis of other biological molecules of interest.

Citation
Susan E. Plunkett, James L. Chao, Thomas J. Tague, and Richard A. Palmer, "Time-Resolved Step-Scan FT-IR Spectroscopy of the Photodynamics of Carbonmonoxymyoglobin," Appl. Spectrosc. 49, 702-708 (1995)
http://www.opticsinfobase.org/as/abstract.cfm?URI=as-49-6-702


Sort:  Journal  |  Reset

References

References are not available for this paper.

Cited By

OSA is able to provide readers links to articles that cite this paper by participating in CrossRef's Cited-By Linking service. CrossRef includes content from more than 3000 publishers and societies. In addition to listing OSA journal articles that cite this paper, citing articles from other participating publishers will also be listed.

« Previous Article  |  Next Article »

OSA is a member of CrossRef.

CrossCheck Deposited