Metastable species of hemoglobin

Room temperature transients and cryogenically trapped intermediates

Research output: Contribution to journalArticle

28 Citations (Scopus)

Abstract

Resonance Raman spectra of photolyzed carbonmonoxyhemoglobin obtained with 10-nanosecond pulses are compared with the spectra of photolyzed carbonmonoxyhemoglobin stabilized at 80 K. In comparing the deoxy with the photodissociated species, the changes in the Raman spectra are the same for these two experimental regimes. These results show that at ambient and cryogenic temperatures the heme pocket in liganded hemoglobin is significantly different from that of deoxyhemoglobin. It is concluded that measurements of the properties of intermediate species from photodissociated hemoglobin stabilized at low temperatures can be used to probe the short-lived metastable forms of hemoglobin present after photodissociation under biologically relevant solution conditions.

Original languageEnglish (US)
Pages (from-to)615-617
Number of pages3
JournalScience
Volume220
Issue number4597
StatePublished - 1983
Externally publishedYes

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Carboxyhemoglobin
Hemoglobins
Temperature
Heme
deoxyhemoglobin

ASJC Scopus subject areas

  • General

Cite this

Metastable species of hemoglobin : Room temperature transients and cryogenically trapped intermediates. / Ondrias, M. R.; Friedman, Joel M.; Rousseau, Denis L.

In: Science, Vol. 220, No. 4597, 1983, p. 615-617.

Research output: Contribution to journalArticle

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AU - Friedman, Joel M.

AU - Rousseau, Denis L.

PY - 1983

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AB - Resonance Raman spectra of photolyzed carbonmonoxyhemoglobin obtained with 10-nanosecond pulses are compared with the spectra of photolyzed carbonmonoxyhemoglobin stabilized at 80 K. In comparing the deoxy with the photodissociated species, the changes in the Raman spectra are the same for these two experimental regimes. These results show that at ambient and cryogenic temperatures the heme pocket in liganded hemoglobin is significantly different from that of deoxyhemoglobin. It is concluded that measurements of the properties of intermediate species from photodissociated hemoglobin stabilized at low temperatures can be used to probe the short-lived metastable forms of hemoglobin present after photodissociation under biologically relevant solution conditions.

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