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BCH210H1 (352)
Lecture

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Department
Biochemistry
Course
BCH210H1
Professor
Michael Baker
Semester
Fall

Description
BCH210H1LECTURE 22Hemoglobin 1Structure2Comparisons with Myoglobin3Oxygenation Cooperativity4Regulation of oxygen bindingFunctions and Regulation of HemoglobinHemoglobin Hb O transporting protein2oO needed for respiration2oCells like amoeba or paramecium dont need circulation since stuff can be transported across cell membraneoLarger animals need circulatory systemTo deliver O and getting rid of waste products like CO22Need efficient O transport and release and no oxidation2oHb fills this roleHb quaternary structure o4 polypeptide subunits2 1 2 1 2Forms tetramer oEach subunit similar to myoglobinMb has a lot ofhelices folds into a spherical structureFor Hb has four spherical structuresEach Hb subunit has heme prosthetic group gives Hb brightly red colour oShownby squares with ball in middleo4 hemes in haemoglobinEssential for O binding22Centre of heme Fe Cu have strong O affinities22Heme has Fe coordinated at centre of protoporphyrin ringoHeme is a disc attached to each Hb subunit4 pyrrole rings5 member rings with N2oFe sits right at the centre of the ringsCoordinates with organic moleculeTo make heme insert Fe into centre of discoIntensely red in colouroTaking disc out of protein will lose red colourCu can also bind to O2oMake blood blue colourPorphyrin ring is flat like a disc oFe in centre coordinated in four coordination links to each N1BCH210H1LECTURE 22oFe is linked to four N of those 4 basic pyrrole structures2Fe has octahedral geometry o8 sides to diamond structure 2oFe has 4 coordination links to N in plane but also has two extra ones at right angles to that planeReally has 6 coordination links 4 are to N of protoporphyrin ringsOther 2 have more significant propertiesoF8 and E72
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