BCH210H1 Lecture Notes - Lecture 5: Myoglobin, Imidazole, Peptide
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BCH210H1 Full Course Notes
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Myoglobin"s interaction with oxygen obeys classical michaelis-menten type substrate saturation behaviour. When myoglobin binds o2 it becomes oxymyoglobin the o2 molecule adds to the heme iron ion as the sixth ligand. Hemoglobin is an 2 2 tetramer each subunit has a virtually identical conformation to mb each of the -chains is in contact with -chains however, few - or - interactions. Hemoglobin resists oxygenation deoxy form is stabilized by specific hydrogen bonds and salt bridges interactions are broken by oxyhemoglobin molecules are stabilized into a new conformation. Deoxyhemoglobin interactions are intact and c-termini of the four subunits are restrained.