Structural and functional properties of a single domain hemoglobin from the food-borne pathogen Campylobactor jejuni

Changyuan Lu, Masahiro Mukai, Yu Lin, Guanghui Wu, Robert K. Poole, Syun Ru Yeh

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26 Scopus citations


Campylobacter jejuni contains two globins, a truncated hemoglobin, Ctb, and a single domain hemoglobin, Cgb. The physiological function of Ctb remains unclear, whereas Cgb has been linked to NO detoxification. With resonance Raman scattering, the iron-histidine stretching mode of Cgb was identified at 251 cm-1. This frequency is unusually high, suggesting an imidazolate character of the proximal histidine as a result of the H-bonding network linking the catalytic triad involving the F8His, H23Glu, and G5Tyr residues. In the CO-complex, two conformers were identified with the νC-O/ νFe-CO at 529/1914 cm-1 and 492/1963 cm-1. The former is assigned to a "closed" conformation, in which the heme-bound CO is stabilized by the H-bond(s) donated from the B10Tyr-E7Gln residues, whereas the latter is assigned to an "open" conformer, in which the H-bonding interaction is absent. The presence of the two alternative conformations demonstrates the plasticity of the protein matrix. In the O 2-complex, the iron-O2 stretching frequency was identified at 554 cm-1, which is unusually low, indicating that the heme-bound O2 is stabilized by strong H-bond(s) donated by the B10Tyr-E7Gln residues. This scenario is consistent with its low O2 off-rate (0.87 s-1). Taken together the data suggest that the NO-detoxifying activity of Cgb is facilitated by the imidazolate character of the proximal F8His and the distal positive polar environment provided by the B10Tyr-E7Gln. They may offer electronic "push" and "pull," respectively, for the O-O bond cleavage reaction required for the isomerization of the presumed peroxynitrite intermediate to the product, nitrate.

Original languageEnglish (US)
Pages (from-to)25917-25928
Number of pages12
JournalJournal of Biological Chemistry
Issue number35
StatePublished - Aug 31 2007

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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