NDLI: Spectral-kinetic heterogeneity in reactions of nitrosyl hemoglobin.

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Spectral-kinetic heterogeneity in reactions of nitrosyl hemoglobin.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Salhany, J. M. Shulman, R. G. Ogawa, S.
Abstract	When NO replaces CO in hemoglobin A in the presence of inositol hexaphosphate, the time course is heterogeneous in contrast to stripped hemoglobin A, where it is homogeneous. If nitrosyl hemoglobin is mixed with inositol hexaphosphate in the stopped-flow apparatus, an extra spectral change is observed which is the cause of the spectral-kinetic heterogeneity in the CO replacement reaction. At wavelengths isosbestic for this extra spectral change, the time courses show an accelerating rate of CO dissociation. On the other hand, the same reaction for NES-des-Arg hemoglobin (hemoglobin reacted with N-ethylmaleimide and carboxypeptidase B) in the presence of inositol hexaphosphate is homogeneous and slow, and shows isosbesty. High-resolution nuclear magnetic resonance spectra indicate that adult nitrosyl hemoglobin in the presence of inositol hexaphosphate is in the low ligand affinity state, thus offering a structural basis for the acceleration observed in the rate of CO dissociation. Hemoglobin Kansas, in the presence of inositol hexaphosphate, which starts and finishes the reaction in the low affinity state, shows a rate of CO dissociation about nine times faster than stripped hemoglobin A. We conclude from these results that (i) the CO to NO replacement reaction can include a functionally important change in the overall conformation of fully liganded hemoglobin, depending on solution conditions and protein type; (ii) the extra spectral change observed for nitrosyl hemoglobin is not the functionally dominating conformational change, but is a secondary effect within the low ligand affinity protein structure; and (iii) the functional properties of heme ligands are largely controlled by two conformational states of the protein, as seen by nuclear magnetic resonance spectroscopy.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	71
Language	English
Publisher	National Academy of Sciences
Publisher Date	1974-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Hemoglobins Analogs & Derivatives Carboxyhemoglobin Carboxypeptidases Ethylmaleimide Hemoglobins, Abnormal Inositol Kinetics Ligands Magnetic Resonance Spectroscopy Nitroso Compounds Phosphates Protein Conformation Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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