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BCHE 395-9 2013 Ligand Binding and Hemoglobin

14 16 co2 not very soluble in aqueous solunon co2

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Unformatted text preview: Curve θ= n [ L] + K d Binding sites occupied = [PL] θ= Total binding sites [PL] + [P] θ= Ka [L] = [L] CooperaNvity: Special Case of Allosteric RegulaNon •  Allosteric protein –  Binding of a ligand to one site affects the binding properNes of a different site, on the same protein –  Can be posiNve or negaNve –  Homotropic •  Normal ligand of the protein is the allosteric regulator –  Heterotropic •  Different ligand affects binding of the normal ligand •  Coopera<vity = posi<ve homotropic regula<on Coopera<vity Leads to a Sigmoid (Allosteric) Binding Curve •  Deoxyhemoglobin: T- state picks up O2 in the lungs, where pO2 is high •  Hb converts into the R- state, so it readily picks up more O2 •  As loaded oxyhemoglobin (R- state) moves back to Nssues, where pO2 is lower, it begins to lose its O2 •  This facilitates the transiNon back to the T- state R-state T-state LU NG [O2]é༎: [CO2]ê༎ OXYGENATED BLOOD (Hb) DEOXYGENATED BLOOD (Hb) CO2 produced as “waste”...
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