2 April 1985 Structure And Reactivity In Hemoglobin: Implications Of Recent Picosecond Transient Raman And Absorption Studies
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Proceedings Volume 0533, Ultrashort Pulse Spectroscopy and Applications; (1985) https://doi.org/10.1117/12.946533
Event: 1985 Los Angeles Technical Symposium, 1985, Los Angeles, United States
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.
© (1985) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
J. M. Friedman, J. M. Friedman, M. R. Ondrias, M. R. Ondrias, E. W. Findsen, E. W. Findsen, S. R. Simon, S. R. Simon, } "Structure And Reactivity In Hemoglobin: Implications Of Recent Picosecond Transient Raman And Absorption Studies", Proc. SPIE 0533, Ultrashort Pulse Spectroscopy and Applications, (2 April 1985); doi: 10.1117/12.946533; https://doi.org/10.1117/12.946533
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