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 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.
Nishiyama
K
K
Department of Chemistry, Virginia Commonwealth University, Richmond 23284.
Hawkridge
F M
FM
D000818:Animals; D002942:Circular Dichroism; D004579:Electron Transport; D066298:In Vitro Techniques; D007700:Kinetics; D008786:Metmyoglobin / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D011487:Protein Conformation; D013816:Thermodynamics; D014907:Whales
C007177:cyanometmyoglobin; D008786:Metmyoglobin