BCHE 395-9 2013 Ligand Binding and Hemoglobin

Shi in hc3 hisdines hemoglobin structure t state

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Unformatted text preview: à༎ High O2 affinity •  O2 binding triggers T to R transi<on •  Involves breaking ion pairs between the α1- β2 interface O2 Binding to Heme: Hb O2 Binding leads to local conformaNonal changes near the heme Deoxygenated Oxygenated R and T States of Hemoglobin: Global ConformaNon Changes in the Hb tetramer Stabilized without oxygen by numerous ion pairs Stabilized by oxygen binding Note shi* in HC3 His/dines! Hemoglobin Structure: T state (Deoxyhemoglobin) Ionic Contacts 8 T- State Subunit InteracNons: Ionic Contact Details LU NG [O2]é༎ pO2 in lungs ~13 kPa DEOXYGENATED BLOOD (Hb) Binds O2 in the lungs pO2 in Nssues ~4 kPa [O2]ê༎ Tiss ues OXYGENATED BLOOD (Hb) Transports O2 to <ssues for respira<on O2 MUST be released in Nssues 10 For effecNve transport O2 affinity must vary with pO2 Two things occurring with O2 binding and transi<on from T to R states: 1.  Oxygen binding affinityñ༏ 2.  Ease of O2 bindingñ༏ 1 kPa = 7.501 torr How can affinity to oxygen change? •  Must be a protein...
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This note was uploaded on 03/02/2014 for the course BIOCHEMIST 395 taught by Professor Potenza during the Spring '14 term at NMSU.

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