The heme environment in barley hemoglobin

Tapan Kanti Das, H. Caroline Lee, Stephen M G Duff, Robert D. Hill, Jack Peisach, Denis L. Rousseau, Beatrice A. Wittenberg, Jonathan B. Wittenberg

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

To elucidate the environment and ligand structure of the heme in barley hemoglobin (Hb), resonance Raman and electron paramagnetic resonance spectroscopic studies have been carried out. The heme is shown to have bis- imidazole coordination, and neither of the histidines has imidazolate character. Barley Hb has a unique heme environment as judged from the Fe-CO and C-O stretching frequencies in the CO complex. Two Fe-CO stretching modes are observed with frequencies at 534 and 493 cm-1, with relative intensities that are pH sensitive. The 534 cm-1 conformer shows a deuterium shift, indicating that the iron-bound CO is hydrogen-bonded, presumably to the distal histidine. A C-O stretching mode at 1924 cm-1 is assigned as being associated with the 534 cm-1 conformer. Evidence is presented that the high Fe-CO and low C-O stretching frequencies (534 and 1924 cm-1, respectively) arise from a short hydrogen bond between the distal histidine and the CO. The 493 cm-1 conformer arises from an open conformation of the heme pocket and becomes the dominant population under acidic conditions when the distal histidine moves away from the CO. Strong hydrogen bonding between the bound ligand and the distal histidine in the CO complex of barley Hb implies that a similar structure may occur in the oxy derivative, imparting a high stability to the bound oxygen. This stabilization is confirmed by the dramatic decrease in the oxygen dissociation rate compared with sperm whale myoglobin.

Original languageEnglish (US)
Pages (from-to)4207-4212
Number of pages6
JournalJournal of Biological Chemistry
Volume274
Issue number7
DOIs
StatePublished - Feb 12 1999

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Carbon Monoxide
Heme
Histidine
Stretching
Hydrogen
Hydrogen bonds
Sperm Whale
Oxygen
Ligands
Hordeum vulgare HB protein
Myoglobin
Deuterium
Electron Spin Resonance Spectroscopy
Hydrogen Bonding
Paramagnetic resonance
Conformations
Iron
Stabilization
Derivatives
Population

ASJC Scopus subject areas

  • Biochemistry

Cite this

Das, T. K., Lee, H. C., Duff, S. M. G., Hill, R. D., Peisach, J., Rousseau, D. L., ... Wittenberg, J. B. (1999). The heme environment in barley hemoglobin. Journal of Biological Chemistry, 274(7), 4207-4212. https://doi.org/10.1074/jbc.274.7.4207

The heme environment in barley hemoglobin. / Das, Tapan Kanti; Lee, H. Caroline; Duff, Stephen M G; Hill, Robert D.; Peisach, Jack; Rousseau, Denis L.; Wittenberg, Beatrice A.; Wittenberg, Jonathan B.

In: Journal of Biological Chemistry, Vol. 274, No. 7, 12.02.1999, p. 4207-4212.

Research output: Contribution to journalArticle

Das, TK, Lee, HC, Duff, SMG, Hill, RD, Peisach, J, Rousseau, DL, Wittenberg, BA & Wittenberg, JB 1999, 'The heme environment in barley hemoglobin', Journal of Biological Chemistry, vol. 274, no. 7, pp. 4207-4212. https://doi.org/10.1074/jbc.274.7.4207
Das TK, Lee HC, Duff SMG, Hill RD, Peisach J, Rousseau DL et al. The heme environment in barley hemoglobin. Journal of Biological Chemistry. 1999 Feb 12;274(7):4207-4212. https://doi.org/10.1074/jbc.274.7.4207
Das, Tapan Kanti ; Lee, H. Caroline ; Duff, Stephen M G ; Hill, Robert D. ; Peisach, Jack ; Rousseau, Denis L. ; Wittenberg, Beatrice A. ; Wittenberg, Jonathan B. / The heme environment in barley hemoglobin. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 7. pp. 4207-4212.
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