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Biochemistry (382)
BCH210H1 (352)
Lecture 5

Lecture 5 allostery in hb and mb

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Department
Biochemistry
Course
BCH210H1
Professor
Stavroula Andreopoulos
Semester
Summer

Description
Lecture 5 Allostery in Hemoglobin and Myoglobin - myoglobin’s interaction with oxygen obeys classical Michaelis-Menten type substrate saturation behaviour - myoglobin polypeptide chain and the α- and β-chains of hemoglobin are composed of 8 α- helical segments denoted the letters A through H - short, unordered regions that connect the helices are names for the segments they connect - successive residues of the helices are numbered - tetrameric nature of Hb is crucial – when a molecule of O binds 2o a heme in Hb, the heme Fe ion is drawn into the plane of the polyphyrin ring – the slight movement sets off a chain of conformational events that are transmitted to adjacent subunits – dramatically enhance the affinity of their heme groups for O 2 - the binding of O t2 one heme of Hb makes it easier for the Hb molecule to bind additional equivalents of O 2 - iron prefers to interact with six ligands – four of which share a common plane – fifth and
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