Structure and ligand selection of hemoglobin II from Lucina pectinata

José A. Gavira, Ana Camara-Artigas, Walleska De Jesús-Bonilla, Juan López-Garriga, Ariel Lewis, Ruth Pietri, Syun-Ru Yeh, Carmen L. Cadilla, Juan Manuel García-Ruiz

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

Lucina pectinata ctenidia harbor three heme proteins: sulfide-reactive hemoglobin I (HbILp) and the oxygen transporting hemoglobins II and III (HbIILp and HbIIILp) that remain unaffected by the presence of H2S. The mechanisms used by these three proteins for their function, including ligand control, remain unknown. The crystal structure of oxygen-bound HbIILp shows a dimeric oxyHbIILp where oxygen is tightly anchored to the heme through hydrogen bonds with Tyr 30(B10) and Gln65(E7). The heme group is buried farther within HbIILp than in HbILp. The proximal His 97(F8) is hydrogen bonded to a water molecule, which interacts electrostatically with a propionate group, resulting in a Fe-His vibration at 211 cm-1. The combined effects of the HbIILp small heme pocket, the hydrogen bonding network, the His97 trans-effect, and the orientation of the oxygen molecule confer stability to the oxy-HbII Lp complex. Oxidation of HbILp Phe(B10) → Tyr and HbIILp only occurs when the pH is decreased from pH 7.5 to 5.0. Structural and resonance Raman spectroscopy studies suggest that HbII Lp oxygen binding and transport to the host bacteria may be regulated by the dynamic displacements of the Gln65(E7) and Tyr 30(B10) pair toward the heme to protect it from changes in the heme oxidation state from FeII to FeIII.

Original languageEnglish (US)
Pages (from-to)9414-9423
Number of pages10
JournalJournal of Biological Chemistry
Volume283
Issue number14
DOIs
StatePublished - Apr 4 2008

Fingerprint

Heme
Hemoglobins
Oxygen
Ligands
Hydrogen
Hydrogen bonds
Hemeproteins
Oxidation
Molecules
Raman Spectrum Analysis
Propionates
Sulfides
Hydrogen Bonding
Ports and harbors
Vibration
Raman spectroscopy
Bacteria
Crystal structure
Water
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Cite this

Gavira, J. A., Camara-Artigas, A., De Jesús-Bonilla, W., López-Garriga, J., Lewis, A., Pietri, R., ... García-Ruiz, J. M. (2008). Structure and ligand selection of hemoglobin II from Lucina pectinata. Journal of Biological Chemistry, 283(14), 9414-9423. https://doi.org/10.1074/jbc.M705026200

Structure and ligand selection of hemoglobin II from Lucina pectinata. / Gavira, José A.; Camara-Artigas, Ana; De Jesús-Bonilla, Walleska; López-Garriga, Juan; Lewis, Ariel; Pietri, Ruth; Yeh, Syun-Ru; Cadilla, Carmen L.; García-Ruiz, Juan Manuel.

In: Journal of Biological Chemistry, Vol. 283, No. 14, 04.04.2008, p. 9414-9423.

Research output: Contribution to journalArticle

Gavira, JA, Camara-Artigas, A, De Jesús-Bonilla, W, López-Garriga, J, Lewis, A, Pietri, R, Yeh, S-R, Cadilla, CL & García-Ruiz, JM 2008, 'Structure and ligand selection of hemoglobin II from Lucina pectinata', Journal of Biological Chemistry, vol. 283, no. 14, pp. 9414-9423. https://doi.org/10.1074/jbc.M705026200
Gavira JA, Camara-Artigas A, De Jesús-Bonilla W, López-Garriga J, Lewis A, Pietri R et al. Structure and ligand selection of hemoglobin II from Lucina pectinata. Journal of Biological Chemistry. 2008 Apr 4;283(14):9414-9423. https://doi.org/10.1074/jbc.M705026200
Gavira, José A. ; Camara-Artigas, Ana ; De Jesús-Bonilla, Walleska ; López-Garriga, Juan ; Lewis, Ariel ; Pietri, Ruth ; Yeh, Syun-Ru ; Cadilla, Carmen L. ; García-Ruiz, Juan Manuel. / Structure and ligand selection of hemoglobin II from Lucina pectinata. In: Journal of Biological Chemistry. 2008 ; Vol. 283, No. 14. pp. 9414-9423.
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