Transient Raman study of hemoglobin

Structural dependence of the iron-histidine linkage

Joel M. Friedman, Denis L. Rousseau, M. R. Ondrias, R. A. Stepnoski

Research output: Contribution to journalArticle

85 Citations (Scopus)

Abstract

Low-frequency resonance Raman spectra of transient hemoglobin species were observed within 10 nanoseconds of photolysis. The Raman frequencies of the iron-proximal histidine stretching mode for transient species having either the R or the T quaternary structure are higher than in the corresponding deoxy species. The observed frequency difference in the iron-histidine mode between the R- and T-state transients indicates that there are quaternary structure-dependent protein forces on the iron-histidine bond in the liganded hemoglobins. These differences are interpreted in terms of changes in the tilt of the histidine with respect to the heme plane.

Original languageEnglish (US)
Pages (from-to)1244-1246
Number of pages3
JournalScience
Volume218
Issue number4578
StatePublished - 1982
Externally publishedYes

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Histidine
Hemoglobins
Iron
Quaternary Protein Structure
Photolysis
Heme

ASJC Scopus subject areas

  • General

Cite this

Transient Raman study of hemoglobin : Structural dependence of the iron-histidine linkage. / Friedman, Joel M.; Rousseau, Denis L.; Ondrias, M. R.; Stepnoski, R. A.

In: Science, Vol. 218, No. 4578, 1982, p. 1244-1246.

Research output: Contribution to journalArticle

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