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Hemoglobin & Myoglobin

That is going to start the conformational change the

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Unformatted text preview: 5 degree between deoxy and oxyhemoglobin - the c entral cavity of deoxy. a little hold and then when oxygen binds you c an no longer see the hole-- there is a change of conformation between the alpha beta axis Size of the central cavity changes on binding oxygen 2/8 and 2/11/13 MCB 2000 Lecture 6 Conformational Change: Oxygenated vs. Deoxygenated Hemoglobin https://iwasa.hms.harvard.edu/project_pages/hemoglobin/hemoglobin.html 2/8 and 2/11/13 MCB 2000 Lecture 6 !"#$%&$'()*G7$80*Z&&$01"2(5*<"73:($2* [732351"2(01(50*$9*42$1"()0*8(17*3&&$01"2(5* '"73:($2* \/31"2)32-*012/51/2"* [$$4"231(:(1-*&"3;0*1$*573)%"*()*5$)9$2#31($)* G(%#$(;3&*'();()%*5/2:"*$2*]()"1(50* * Difference between hemoglobin and mygolbin besides the stucture? - because hemogolbin has 4 subunits and each of them can bind to heme - when oxygen binds to the fi rst heme in one of the subunits that is going to start the conformational change - the binding to oxgyen to one subunit will effect the binding of the next subunit becuase of the change in conformation - this will be translated across the entrire molecule. becuase mygolbin doesn't have any partners will not show this behavior - this is called cooperativity the subunits of hemogolbin are interactive and when oxgyen binds they show cooperativity - communication between subunits. Q uaternary - leads to cooperativity - which leads to sigmoidal curve 2/8 and 2/11/13 MCB 2000 Lecture 6 Compare the oxygen binding curves for hemoglobin and myoglobin Note the different shapes of each curve: Mb is hyperbolic Hb is sigmoidal (Sshaped) Degree of staturation with myoglobin and hemoglobin - 0.5 Y - straight line and then drop line down - this s hows the releavent something - lower partial pressure - the S shape for hemoglobin becuase of c opperavity - myoglobin will never give you an Sshaped curve) because lackcopperativiety because only has one subunit need mult. subunit to have c orperativity. 2/8 and 2/11/13 MCB 2000 Lecture 6 Deoxy hemoglobin - the T state - less advice state (tight) The R state - exsist with oxygenated hemoglobin - more active and Relaxed state (R) Sigmoid shape of oxygen saturation curve indicates cooperativity between subunits in binding oxygen 2/8 and 2/11/13 Binding of oxygen to one subunit disrupts some noncovalent interactions while forming new ones. Alteration in conformation makes it easier for oxygen to bind to other subunits. MCB 2000 Lecture 6 !$8*;$"0*17"*$F-%")*;(00$5(31($)*5/2:"* 2"&31"*1$*;"&(:"2-*$9*$F-%")*()*17"*'$;-V* Hemoglobin - trasnport oxygen and myogolbin - store oxygen - rely only on myoglobin - our tissue would not get enough oxygen - partial pressure in the lungs - myoglobin has only released 7% of its oxygen - not good when taking about aerobic respiration where hemoglobin will release 66% of its oxygen at the s ame partial pressure - myo...
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