Question

In: Chemistry

Synthesis of a Cobalt Complex that Mimics Oxygen Binding in Hemoglobin Knowing the decrease in volume...

Synthesis of a Cobalt Complex that Mimics Oxygen Binding in Hemoglobin

Knowing the decrease in volume at ambient temperature and atmospheric pressure, the number of moles of O2 absorbed per mole of Co(salen) can be calculated.

From your oxygen uptake experiments, how many equivalents of oxygen are bound to the cobalt? Draw the structure of your proposed molecule (you will need to know the amount of Co(salen) you added to the sidearm flask and the change of volume you observed – show your work).

0.05 g of Co(salen) was added to the sidearm flask and a change of volume of 2 mL was observed.

Solutions

Expert Solution

Basically the "Red" form of salen is capable of complexing with Oxygen that actually mimcs the Oxyhaemoglobin structure.

The d7 state of Co Can exist as a High/Low spin Complex.

thus, applying the law of chemical equivalence to the above change in oxidation state of Co before and after combining with O2 molecule we have,

NCo * VCo = NO2 * VO2

Equivalents of O2 Molecules are bound to 0.05g of Cobalt.


Related Solutions

Synthesis of a Cobalt Complex that Mimics Oxygen Binding in Hemoglobin Co(II) salen complex Explain what...
Synthesis of a Cobalt Complex that Mimics Oxygen Binding in Hemoglobin Co(II) salen complex Explain what happens when the oxygen adduct is dissolved in chloroform. Would the results be different if the reaction was performed in dichloromethane rather than DMSO? What about in acetonitrile?
List positive and negative effectors for oxygen binding to hemoglobin. explain cooperative binding using hemoglobin as...
List positive and negative effectors for oxygen binding to hemoglobin. explain cooperative binding using hemoglobin as an example. Correlate the NCI involved in stabilizing Hb’s and Mb’s structures. please answer all
Describe the relationship between the partial pressure of oxygen and the binding of oxygen to hemoglobin.
Describe the relationship between the partial pressure of oxygen and the binding of oxygen to hemoglobin.
Hemoglobin and Myoglobin, HOW is oxygen binding regulated? what other mechanisms control oxygen binding in oxygenated...
Hemoglobin and Myoglobin, HOW is oxygen binding regulated? what other mechanisms control oxygen binding in oxygenated vs deoxygenated tissues ( lung v. exercising muscles)?  
Which of the following will decrease the affinity of oxygen for hemoglobin at low oxygen partial...
Which of the following will decrease the affinity of oxygen for hemoglobin at low oxygen partial pressures and shift the oxyhemoglobin saturation curve to the right, resulting in increased oxygen unloading for active tissues? Select one: a. high CO2 b. low H+ c. low temperature d. high hemoglobin levels e. low CO2
Gas Transport in the Blood. Efficient oxygen exchange requires the reversible binding of oxygen to hemoglobin....
Gas Transport in the Blood. Efficient oxygen exchange requires the reversible binding of oxygen to hemoglobin. Describe the relationship between the partial pressure of oxygen in the blood and the oxygen saturation of hemoglobin. Include a labeled figure that clearly shows this relationship. Then, explain in detail the significance of the relationship by discussing what is seen in “average” body tissues and tissues that are metabolically active (name them). Then, explain in detail the significance of the relationship with respect...
Gas Transport in the Blood. Efficient oxygen exchange requires the reversible binding of oxygen to hemoglobin....
Gas Transport in the Blood. Efficient oxygen exchange requires the reversible binding of oxygen to hemoglobin. Describe the relationship between the partial pressure of oxygen in the blood and the oxygen saturation of hemoglobin. Include a labeled figure that clearly shows this relationship. Then, explain in detail the significance of the relationship by discussing what is seen in “average” body tissues and tissues that are metabolically active (name them). Then, explain in detail the significance of the relationship with respect...
Biochemistry. Please explain: the structure and oxygen binding mechanism of myogloblin and hemoglobin.
Biochemistry. Please explain: the structure and oxygen binding mechanism of myogloblin and hemoglobin.
What role does the hydrogen peroxide play in the synthesis of a Pentammino Complex of Cobalt(III)...
What role does the hydrogen peroxide play in the synthesis of a Pentammino Complex of Cobalt(III) Chloride [Co(NH3)5Cl]Cl2, Pentamminenitro- and Nitritro- Cobalt(III) Chloride
What other factors will promote oxygen release from hemoglobin? What factors promote binding of oxygen to...
What other factors will promote oxygen release from hemoglobin? What factors promote binding of oxygen to hemoglobin? High levels of CO2 will promote oxygen release/binding (Pick one). Explain in terms of metabolic pathways why high levels of CO2 would promote release/binding of oxygen How does the protein sequence of hemoglobin differ from normal hemoglobin? How does this change affect the structure of the protein? Explain what happens on the protein level to cause the sickling of the Red blood cells.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT