Myoglobin
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Myoglobin transports oxygen from capillaries to mitochondria in muscle tissue. It contains a heme group that can bind one oxygen molecule to form oxymyoglobin. Oxygen binds to the iron atom of the heme group through hydrophobic and histidine interactions. Myoglobin binds oxygen noncooperatively, as shown by its hyperbolic titration curve, and has a higher affinity for oxygen than hemoglobin due to its lower p50 value.
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![Oxygen binds to myoglobin using a
noncooperative interaction
Mb + O2 = Mb-O2 Keq = ([Mb] [O2]) / [Mb-O2]
Myoglobin’s p50 value (K) is lower than that of
hemoglobin; therefore myoglobin has a
higher binding affinity for oxygen ](https://image.slidesharecdn.com/myoglobin-150209212223-conversion-gate02/85/Myoglobin-5-320.jpg)
Myoglobin
- 1. O2 & CO2 Transport and Exchange Camille Renee Dr. S.D. BCHM1 2101 STV Saint James School of Medicine
- 2. • α-helical secondary structure • Contains one heme group in its internal hydrophobic cleft and therefore can bind one oxygen molecule, forming oxymyoglobin • Oxygen binds to ferrous iron atom on heme group. This binding is stabilized by hydrophobic interactions and a nitrogen atom derived from histidine • Transports oxygen from capillaries to mitochondria in working tissue
- 3. Myoglobin’s hyperbolic titration curve represents its lack of allosteric interactions
- 5. Oxygen binds to myoglobin using a noncooperative interaction Mb + O2 = Mb-O2 Keq = ([Mb] [O2]) / [Mb-O2] Myoglobin’s p50 value (K) is lower than that of hemoglobin; therefore myoglobin has a higher binding affinity for oxygen
- 7. 1. Blood chemistry. D.S. (2014). BCHM1 2101 STV. Saint James School of Medicine. 2. Myoglobin. Wikipedia. (2014). http://upload.wikimedia.org/wikipedia/commons/thumb/6/60/Myogl obin.png/592px-Myoglobin.png