1 Each myoglobin molecule has one heme group and can bind one oxygen molecule. Hemoglobin on the other hand can bind up to 4 molecules of oxygen.
Both Myoglobin and Haemoglobin binds to oxygen, but they differ in many aspects. Usual site: Myoglobin: muscle tissues Haemoblogin: red blood cells (whole body) Main function: Myoglobin: stores oxygen (in muscle tissues) Haemoglobin: Oxygenation of tissues (whole body) Waste (CO2) collection (whole body) gas exchange (lungs, tissues) Oxygen carrying capacity: Myoglobin: monomeric = one heme prosthetic group, one iron atom Haemoglobin: tetrameric = four heme prosthetic groups, four iron atoms. Structure Myoglobin: secondary and tertiary, no allosteric interaction Haemoglobin: quaternary structure, allosteric interaction, different affinity Affinity to oxygen Myoglobin: Oxidation (Fe2+ → Fe3+) prevents oxygen binding. Haemoglobin: requirement specific affinity: (gradually increasing in the lungs, . gradually decreasing at the tissues) Prefered binding Myoglobin: Carbon monoxide preferred to Oxygen. Haemoglobin: Oxygen, carbon dioxide While in cases of hugely increased demand, myoglobin releases oxygen for metabolism, but, in the long run haemoglobin is more suitable for the purpose.
Five molecules of H2SO4 contains 20 atoms of Oxygen
One oxygen molecule has two oxygen atoms.
There are 2 atoms and 3 molecules in oxygen.
That depends on the fuel. Natural gas, methane, needs 2 molecules of oxygen, but gasoline, octane, needs 17 molecules of oxygen.
Haemoglobin combines with four molecules of oxygen.
Both Myoglobin and Haemoglobin binds to oxygen, but they differ in many aspects. Usual site: Myoglobin: muscle tissues Haemoblogin: red blood cells (whole body) Main function: Myoglobin: stores oxygen (in muscle tissues) Haemoglobin: Oxygenation of tissues (whole body) Waste (CO2) collection (whole body) gas exchange (lungs, tissues) Oxygen carrying capacity: Myoglobin: monomeric = one heme prosthetic group, one iron atom Haemoglobin: tetrameric = four heme prosthetic groups, four iron atoms. Structure Myoglobin: secondary and tertiary, no allosteric interaction Haemoglobin: quaternary structure, allosteric interaction, different affinity Affinity to oxygen Myoglobin: Oxidation (Fe2+ → Fe3+) prevents oxygen binding. Haemoglobin: requirement specific affinity: (gradually increasing in the lungs, . gradually decreasing at the tissues) Prefered binding Myoglobin: Carbon monoxide preferred to Oxygen. Haemoglobin: Oxygen, carbon dioxide While in cases of hugely increased demand, myoglobin releases oxygen for metabolism, but, in the long run haemoglobin is more suitable for the purpose.
4 Hb has four peptide in total, 2-2 each of alpha and beta chain, each of the four chain has heme group bind to it which carry iron moiety , now in total 4 iron moiety, ecah of which can bind one O2 molecule , thus answer is 4, if talking about atoms it would be 4*2 =8 atoms ....
23 moles of oxygen contain 138,509.10e23 molecules.
Air is 21% oxygen so 21% of 200 is 42 oxygen molecules.
2
4 molecules of oxygen - one to each subunit on the heme
20 hydrogen 10 oxygen
For what purpose?
Five molecules of H2SO4 contains 20 atoms of Oxygen
With the production of one molecule of sugar six molecules of oxygen are produced during photosynthesis.
2 water molecules form one molecule of oxygen.