Heme Biochem 1 Fn

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Myoglobin

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tert histadine structure includes Fe-heme and bind to O2 more tightly Hb

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allosteric interactionn (O2 -heme)

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binding of a molecule to a binding site affects binding properties of another site on the protein.

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prosthetic group (Fe-heme)

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non-protein permanently associated with the protein

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CO-Hb in smokers

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CO2 bind to Fe2+ more tightly than O2 --- CO bind to Fe2+ strongest (straighter) ---- nonsmoker 1% vs 10% of CO in smoker

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MetHb (Fe3+)

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is oxidated from "normal" Fe2+ --- can't bind to O2 and CO2 --- only bind to CN --

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R state relax have more room to hold on ..........

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Oxygen

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Hb O2 binding cooperativity

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bind one and then all 4

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Myosin - Hb Oxygen binding curve

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Muscle Myo bind more than Hb ----- lung bind the same

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BPG is -2 in LOW pH (His is POSitve) will ......

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bind to His stronger than O2 --- low pH = high CO2

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BPG is -2 in HIGH pH (His is NEUtral) will ......

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not bind to Hb and O2 will take over

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Acidosis vs alkalosis

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COPD (too much CO2 in blood) vs hyperventilation (too much O2 in blood - high pH - BPD can't kick out O2 for brain to use)

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HbF vs HbA

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HbF bind to O2 stronger (less aff to BPF) than HbA and act like Myoglobin to take O2 from O2

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Tay-Sachs diseases

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Hexo-saminidase-A (accumulate lipid on brain)

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Met-Hb (Fe3+) is a "spontaneous" products of .....

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Fe2+ ---- it does not bind oxygen but Cyanide (which doesn't bind to Hb-Fe2) ------------------ P

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Amyl nitrite is used to treat ....... (metHb good side)

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cyanide poisoning by converting Hb-Fe2 to metHb-Fe3 (Cyanide will release Fe-Cu center in site 4 of ETC and bind to metHbFe3) Nitrite will oxidize (take an e) Fe2 to Fe3

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cyanide poisoning

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cyanide will bind to Fe-Cu center sub unit in Site 4 and prevent Cyt C enzyme from passing e- to O2 (via Fe-Cu) --> can't use O2 ETC is shut down at site 4

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When oxygen binds to a heme-containing protein, the two open coordination bonds of Fe2+ are occupied by:

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one O2 molecule and one amino acid atom.

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Myoglobin and the subunits of hemoglobin have

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very similar tertiary structures, but different primary structures

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The interactions of ligands with proteins

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are usually transient - transferable.

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In the binding of oxygen to myoglobin, the relationship between the concentration of oxygen and the fraction of binding sites occupied can best be described as

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hyperbolic.