A resonance Raman study of the temperature dependence of ligand photolysis and recombination in hemoglobins

M. R. Ondrias, T. W. Scott, Joel M. Friedman, V. W. Macdonald

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

Transient Raman spectroscopy has been used to study geminate recombination in photolyzed hemoglobins at cryogenic temperatures. The temperature dependence of the deoxy heme survival probability during a 10 ns photolysis event is analyzed in terms of a distribution of energy barriers. Studies employing different ligands (CO, O2, NO), and a mutant hemoglobin (hemoglobin Zurich) demonstrates that the barriers controlling rebinding at early times are both and protein specific.

Original languageEnglish (US)
Pages (from-to)351-355
Number of pages5
JournalChemical Physics Letters
Volume112
Issue number4
DOIs
StatePublished - Dec 14 1984
Externally publishedYes

Fingerprint

Photolysis
hemoglobin
photolysis
Hemoglobins
Ligands
temperature dependence
ligands
Energy barriers
Carbon Monoxide
Heme
Cryogenics
Raman spectroscopy
cryogenic temperature
Temperature
proteins
Proteins
energy
hemoglobin Zurich

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Condensed Matter Physics
  • Atomic and Molecular Physics, and Optics
  • Surfaces and Interfaces

Cite this

A resonance Raman study of the temperature dependence of ligand photolysis and recombination in hemoglobins. / Ondrias, M. R.; Scott, T. W.; Friedman, Joel M.; Macdonald, V. W.

In: Chemical Physics Letters, Vol. 112, No. 4, 14.12.1984, p. 351-355.

Research output: Contribution to journalArticle

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