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...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the American Chemical Society 2004-03, Vol.126 (9), p.2682-2683
Main Authors: Samuni, Uri, Ouellet, Yannick, Guertin, Michel, Friedman, Joel M, Yeh, Syun-Ru
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Bacterial Proteins - chemistry
Biological and medical sciences
Fundamental and applied biological sciences. Psychology
Hemoglobins - chemistry
Hemoproteins
Metalloproteins
Models, Molecular
Mycobacterium tuberculosis - chemistry
Protein Conformation
Proteins
Spectrum Analysis, Raman
Truncated Hemoglobins
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja038093i