Intrinsic fluorescence emission of intact oxy hemoglobins

Rhoda Elison Hirsch, R. Suzanne Zukin, Ronald L. Nagel

Research output: Contribution to journalArticle

82 Citations (Scopus)

Abstract

Fluorescence has not been previously detected in intact hemoproteins. We have been able to measure significant fluorescence emission in purified oxy HbA using front-face fluorometry. The excitation maximum (293 nm), the emission maximum (325 nm) and the fluorescence spectra of Hb Rothschild (β 37 Trp → Arg) allows us to conclude that β 37 Trp is primarily responsible for the fluorescence signal of HbA. We propose that this intrinsic fluorescence of hemoglobin may be used as a probe to study conformational changes in hemoglobin and possibly other heme-containing proteins.

Original languageEnglish (US)
Pages (from-to)432-439
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume93
Issue number2
DOIs
StatePublished - Mar 28 1980

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Hemoglobins
Fluorescence
Fluorometry
Heme
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Intrinsic fluorescence emission of intact oxy hemoglobins. / Hirsch, Rhoda Elison; Zukin, R. Suzanne; Nagel, Ronald L.

In: Biochemical and Biophysical Research Communications, Vol. 93, No. 2, 28.03.1980, p. 432-439.

Research output: Contribution to journalArticle

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