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. 1992 Dec 1;89(23):11371–11375. doi: 10.1073/pnas.89.23.11371

Vibronic energy map and excited state vibrational characteristics of magnesium myoglobin determined by energy-selective fluorescence.

A D Kaposi 1, J M Vanderkooi 1
PMCID: PMC50552  PMID: 1454822

Abstract

The vibrational frequencies of the singlet excited state of Mg-substituted myoglobin and relative absorption probabilities were determined by fluorescence line-narrowing spectroscopy. These spectra contain information on the structure of the excited state species, and the availability of vibrationally resolved spectra from excited state biomolecules should aid in elucidating their structure and reactivity.

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Selected References

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  1. Angiolillo P. J., Leigh J. S., Jr, Vanderkooi J. M. Resolved fluorescence emission spectra of iron-free cytochrome c. Photochem Photobiol. 1982 Aug;36(2):133–137. doi: 10.1111/j.1751-1097.1982.tb04354.x. [DOI] [PubMed] [Google Scholar]
  2. Campbell B. F., Chance M. R., Friedman J. M. Linkage of functional and structural heterogeneity in proteins: dynamic hole burning in carboxymyoglobin. Science. 1987 Oct 16;238(4825):373–376. doi: 10.1126/science.3659921. [DOI] [PubMed] [Google Scholar]
  3. Eagles J., Fairweather-Tait S. J., Portwood D. E., Self R., Götz A., Heumann K. G. Comparison of fast atom bombardment mass spectrometry and thermal ionization quadrupole mass spectrometry for the measurement of zinc absorption in human nutrition studies. Anal Chem. 1989 May 1;61(9):1023–1025. doi: 10.1021/ac00184a021. [DOI] [PubMed] [Google Scholar]
  4. Fidy J., Vanderkooi J. M., Zollfrank J., Friedrich J. More than two pyrrole tautomers of mesoporphyrin stabilized by a protein. High resolution optical spectroscopic study. Biophys J. 1992 Feb;61(2):381–391. doi: 10.1016/S0006-3495(92)81844-1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Ormos P., Ansari A., Braunstein D., Cowen B. R., Frauenfelder H., Hong M. K., Iben I. E., Sauke T. B., Steinbach P. J., Young R. D. Inhomogeneous broadening in spectral bands of carbonmonoxymyoglobin. The connection between spectral and functional heterogeneity. Biophys J. 1990 Feb;57(2):191–199. doi: 10.1016/S0006-3495(90)82522-4. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Vanderkooi J. M., Moy V. T., Maniara G., Koloczek H., Paul K. G. Site-selected fluorescence spectra of porphyrin derivatives of heme proteins. Biochemistry. 1985 Dec 31;24(27):7931–7935. doi: 10.1021/bi00348a013. [DOI] [PubMed] [Google Scholar]

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