Anomalous azide binding to metmanganomyoglobin.
The reaction of metmanganomyoglobin (MnIIIMb) with azide presents a novel pattern with direct evidence for kinetic complexity. Although the kinetic analysis may not be unique, it appears that the azide complex cannot be fully formed, as judged by spectrophotometric changes, even with an infinitely great [N3-]. This is interpreted as resulting from an equilibrium between the final spectroscopically observable azide complex and an intermediate species whose spectrum is not substantially different from that of MnIIIMb itself. The two forms of the azide complex appear to exhibit roughly equal proportions at 3 degrees C. We propose that this intermediate is a weak Mn3+ -azide complex in which the metal ion remains out-of-plane toward the imidazole of the proximal histidine, but that the metal lies toward the anion in the "final" complex.
D000818:Animals; D001386:Azides; D001665:Binding Sites; D007700:Kinetics; D008297:Male; D008345:Manganese; D008433:Mathematics; D009211:Myoglobin; D011485:Protein Binding; D011487:Protein Conformation; D014907:Whales
D001386:Azides; D009211:Myoglobin; D008345:Manganese