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Proceedings Paper

Structure And Reactivity In Hemoglobin: Implications Of Recent Picosecond Transient Raman And Absorption Studies
Author(s): J. M. Friedman; M. R. Ondrias; E. W. Findsen; S. R. Simon
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Paper Abstract

Recent picosecond transient absorption studies' show that the yield of geminate rebinding is sensitive to protein structure. Picosecond transient Raman studies 2 reveal that over the time course (T = 200 ps) of the geminate rebinding, the effective tertiary structure about the heme is not relaxing. The results of this study also imply strong coupling among the elements of tertiary structure that control both the frequency of iron-proximal histidine stretching motion and the ligand binding properties of the heme. These findings and conclusions are used to further develop a working model in which reactivity and structure about the heme are controlled by an effective tertiary structure associated with what Karplus and co-workers3 call an "allosteric core" comprised of the heme, the proximal histidine (F-8), a portion of the F-helix and the a1-B2 interface.

Paper Details

Date Published: 2 April 1985
PDF: 7 pages
Proc. SPIE 0533, Ultrashort Pulse Spectroscopy and Applications, (2 April 1985); doi: 10.1117/12.946533
Show Author Affiliations
J. M. Friedman, AT&T Bell Laboratories (United States)
M. R. Ondrias, University of New Mexico (United States)
E. W. Findsen, University of New Mexico (United States)
S. R. Simon, SUNY at Stony Brook (United States)

Published in SPIE Proceedings Vol. 0533:
Ultrashort Pulse Spectroscopy and Applications
M. J. Soileau, Editor(s)

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