BCH210H1 Chapter Notes - Chapter 6: Myoglobin, Heme, Hemoglobin
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BCH210H1 Full Course Notes
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Document Summary
Myoglobin: monomeric, 8 alpha helices protein, the heme fits into a 3d pocket/cleft inside the monomer protein, held together by non-covalent interactions, the pocket/cleft is hydrophobic. Red blood cells: contain a large amount of hemoglobin molecules in each blood cell, 3x108 hb molecules in each cell, constitutes 90% of the intracellular protein. Deoxyhemoglobin: not bound to o2: each hemoglobin can carry four oxygen molecules, alpha chains and beta chains have extensive interactions via non-covalent forces. O2 binding to heme: his-93 (proximal near-by histidine) the n atom on the imidazole ring crates the fifth ligand. Reading 7: cleft: it is hydrophobic due to the presence of. Phe-43 and val-68 residues: if we were to take the heme into an aqueous solution it will covert the iron into fe3+ (ferric iron) Purified heme does not bind to o2 reversibly: hydrophobic cleft partially transfers the electrons to the.
