Hemoproteins PDF
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Cairo University Medicine
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Summary
This document discusses the structures and functions of hemoproteins. It covers heme structure, the connection to proteins (myoglobin and hemoglobin), and the oxygen-carrying aspects. The text further expands to explore the cooperative binding and dissociation properties of hemoglobin, highlighting factors like pH, and the allosteric effectors governing its function and explaining how these relate to blood.
Full Transcript
central metal is iron 4 pyrrole > - 1 porphyrin primaily for proteins that contain heme and are associated withO storage and transport O, stagine hasport of G from...
central metal is iron 4 pyrrole > - 1 porphyrin primaily for proteins that contain heme and are associated withO storage and transport O, stagine hasport of G from Lissue and - CO. ung + A - H Fett in home is bound to kinlidine Fortanchoe home to the prokin 2 propionale side chair on the heme project outward ↳ soluble , stabilizing it interaction with the protein without heme 3. Iron stabilization : keeps if an Fe"/Fe - > inhibits Or binding 4. Decreased CO affinity : without this mechanism > - CO would out- compete Or (it binds more shongly Distal Histidine stabilizes Oz binding by creating steric hindrance ↳ prevents CO from binding > - ↓ COaffinity. 5 O2 binding to 1 heme - increases affinity of remaining heme sites for 02 to maintain plt in blood ~ essential for role in Or delivery allows Ab ho S change shope dening O binding 5-form : Jense o low ↳ affinity for 02 R- form : Relaxed > - rotation of 150 T-for 10 R-for affinity bind sites ↳ to increasing O2 in remaining affinity for. high 0 Cooperative binding - Or binding to 1 heme site ↳ increases affinity to the other sites for 02 ↳ signoidal O2 dissociation curve Wann ? ( pulled place Fe e into the > less rigid +more sith - - - for to R-fom > - CO2 is exheled to Hb releases H + - facilitates Or binding
