Structure and reactivity in hemoglobin: implications of recent picosecond transient raman and absorption studies

J. M. Friedman, M. R. Ondrias, E. W. Findsen, S. R. Simon

Research output: Contribution to journalArticle

1 Scopus citations

Abstract

Recent picosecond transient absorption studies1 show that the yield of geminate rebinding is sensitive to protein structure. Picosecond transient Raman studies2 reveal that over the time course (Շ ≃ 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-workers3call an "allosteric core" comprised of the heme, the proximal histidine (F-8), a portion of the F-helix and the α12 interface.

Original languageEnglish (US)
Pages (from-to)8-14
Number of pages7
JournalProceedings of SPIE - The International Society for Optical Engineering
Volume533
DOIs
StatePublished - Apr 3 1985
Externally publishedYes

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials
  • Condensed Matter Physics
  • Computer Science Applications
  • Applied Mathematics
  • Electrical and Electronic Engineering

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