Metastable photoproducts from carbon monoxide myoglobin

Denis L. Rousseau, P. V. Argade

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

The photoproduct of carbon monoxide myoglobin generated at 4 K and lower has a resonance Raman spectrum characteristic of a high-spin heme but in which the high-frequency core size-sensitive lines are at lower frequency than those in the deoxy preparation. Such differences are not detected in the photoproduct generated at higher temperatures (50 K) or in that generated at room temperature with 10-nsec pulses. The data indicate that at the low temperature (4 K), the heme in the photoproduct is not fully relaxed, and from the data we conclude that the photoproduct has an expanded porphyrin core. We infer that the core size exceeds that in deoxymyoglobin because the rigid protein prevents the high-spin iron atom from moving to its full out-of-plane displacement at the very low temperatures.

Original languageEnglish (US)
Pages (from-to)1310-1314
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume83
Issue number5
StatePublished - 1986
Externally publishedYes

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Myoglobin
Carbon Monoxide
Temperature
Heme
Porphyrins
Iron
Proteins

ASJC Scopus subject areas

  • General
  • Genetics

Cite this

Metastable photoproducts from carbon monoxide myoglobin. / Rousseau, Denis L.; Argade, P. V.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 83, No. 5, 1986, p. 1310-1314.

Research output: Contribution to journalArticle

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