Kinetics of Conformation Change in Cyanometmyoglobin Following Electron Transfer Monitored by Magnetically Induced Circular Dichroism Spectrometry

The characterization of the dynamics of conformational changes that accompany the ligand binding and dissociation reactions of myoglobin may provide insights into the events that control the physiological function of this oxygen storage protein. The cyanometmyoglobin system was chosen for this study...

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Veröffentlicht in:Biochemical and biophysical research communications 1994-12, Vol.205 (3), p.1724-1728
Hauptverfasser: Nishiyama, K., Hawkridge, F.M.
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description The characterization of the dynamics of conformational changes that accompany the ligand binding and dissociation reactions of myoglobin may provide insights into the events that control the physiological function of this oxygen storage protein. The cyanometmyoglobin system was chosen for this study because cyanide binds to the metmyoglobin state and dissociates upon reduction. The potential step spectroelectrochemical method was used here because the rate of cyanometmyoglobin reduction at an electrode can be controlled so that the rate of dissociation of the reduced cyanomyoglobin can then be followed.
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subjects Animals
Circular Dichroism
Electron Transport
In Vitro Techniques
Kinetics
Metmyoglobin - analogs & derivatives
Metmyoglobin - chemistry
Metmyoglobin - metabolism
Oxidation-Reduction
Protein Conformation
Thermodynamics
Whales
title Kinetics of Conformation Change in Cyanometmyoglobin Following Electron Transfer Monitored by Magnetically Induced Circular Dichroism Spectrometry
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