The absence of proximal strain in the truncated hemoglobins from Mycobacterium tuberculosis.
HbN and HbO are two truncated hemoglobins from Mycobacterium tuberculosis. Resonance Raman spectra of the deoxy derivatives of these two homodimeric hemoglobins indicate that there is no proximal strain imposed by intersubunit interactions on the proximal iron-histidine bond as that observed in the tetrameric human hemoglobin. In addition, with nanosecond laser flash photolysis, it was concluded that movement along the Fe-His bond following the dissociation of CO does not trigger a quaternary structural transition in these two hemoglobins.
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA.
Uri
U
Samuni
Yannick
Y
Ouellet
Michel
M
Guertin
Joel M
JM
Friedman
Syun-Ru
SR
Yeh
D001426:Bacterial Proteins / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D008958:Models, Molecular; D009169:Mycobacterium tuberculosis / Q000737:chemistry*; D011487:Protein Conformation; D013059:Spectrum Analysis, Raman; D054793:Truncated Hemoglobins
D001426:Bacterial Proteins; D006454:Hemoglobins; D054793:Truncated Hemoglobins