it is learned that oxygen keeps us alive! how it works in our body?what quality oxygen have for this?

Answer 1

Oxygen is needed by our body in order to sustain life. Oxygen is carried and used by (RBC) red blood cells, one of the most important cellular elements in our body. Through these cells, oxygen circulates around the body and allows the basic , vital functions to proceed normally. Oxygen is utilised in almost all biochemical reactions occurring inside; life won't be sustained without it.

Answer 2

good question my firend .there are two respirations in our body they are as we all know inhaling the fresh air into the lungs.and the other one is as the most of the biologists know oxydative respiration .which is basically an energy synthesizing machinary present in the mitochondrial organelle in our all body cells .where oxygen plays a key role as an electron acceptor.our respired oxygen's first duty is to accept the electrons and then it forms a water molecule.if this electron transport chain breaks withou oxygen within some minutes we may die.refer (ETC-electron transport chain in any biology book from school to college and above.right?

Answer 3

good question my firend .there are two respirations in our body they are as we all know inhaling the fresh air into the lungs.and the other one is as the most of the biologists know oxydative respiration .which is basically an energy synthesizing machinary present in the mitochondrial organelle in our all body cells .where oxygen plays a key role as an electron acceptor.our respired oxygen's first duty is to accept the electrons and then it forms a water molecule.if this electron transport chain breaks withou oxygen within some minutes we may die.refer (ETC-electron transport chain in any biology book from school to college and above.right?

Answer 4

Oxygen is needed by our body in order to sustain life. Oxygen is carried and used by (RBC) red blood cells. Through these cells, oxygen circulates around the body and allows the basic , vital functions to proceed normally. Oxygen is utilised in almost all biochemical reactions occurring inside.It inhale by nose and go to lungs then CO2 gas expelled by lungs.the oxygen carrying capacity of RBC is play imp role in function of body organ

Answer 5

Its not that oxygen has a quality, its that our body is set up to utilize oxygen.

We breathe it in, our lungs absorb it, pass it into our blood stream and throughout our bodies, our organs, brain, heart, etc. Fortunately, it works and it keeps us alive.

Answer 6

Experimentally: interior the previous due seventeenth century, Robert Boyle proved that air is major for combustion. English chemist John Mayow subtle this artwork with techniques from showing that fireside calls for in elementary words component to air that he suggested as spiritus nitroaereus or only nitroaereus.[fifty 3] in a unmarried try he got here upon that putting both a mouse or a lit candle in a closed container over water led to the water to upward thrust and replace one-fourteenth of the air's volume previously extinguishing the topics.[fifty 4] From this he surmised that nitroaereus is ate up in both respiration and combustion. Oxygen replaced into independently got here across with techniques from Joseph Priestley in Wiltshire, in 1774, and Carl Wilhelm Scheele, in Uppsala, a 365 days previously, yet Priestley is frequently given precedence because he revealed his findings first. If the question is about somewhat oxigen, then we ought to got here across it when we got here around the element O2.

Answer 7

For every work we need energy. even for working of heart. oxygen provides us this energy. we inhales it through nose .than it reaches to lungs through nostrils and than it is absorbed by the blood.through blood it reaches all the body organs.then this oxygen is absorbed by cells and provides energy by reacting with glycogen.

Answer 8

Oxygen entering the lungs enters the blood and fuses to form oxy haemoglobin.
Hemoglobin or haemoglobin [frequently abbreviated as Hb or Hgb] is the iron-containing oxygen-transport metalloprotein in the red cells of the blood in mammals and other animals. Hemoglobin in vertebrates transports oxygen from the lungs to the rest of the body, such as to the muscles, where it releases the oxygen load. Hemoglobin also has a variety of other gas-transport and effect-modulation duties, which vary from species to species, and which in invertebrates may be quite diverse.
The hemoglobin molecule in humans is an assembly of four globular protein subunits. Each subunit is composed of a protein chain tightly associated with a non-protein heme group
Oxyhemoglobin contains iron formally in its +3 oxidation state while deoxyhemoglobin contains iron in the +2 oxidation state.

Assigning oxygenated hemoglobin's oxidation state is difficult because oxyhemoglobin is diamagnetic (no net unpaired electrons), but the low-energy electron configurations in both oxygen and iron are paramagnetic. Triplet oxygen, the lowest energy oxygen species, has two unpaired electrons in antibonding π* molecular orbitals. Iron(II) tends to be in a high-spin configuration where unpaired electrons exist in eg antibonding orbitals. Iron(III) has an odd number of electrons and necessarily has unpaired electrons. All of these molecules are paramagnetic (have unpaired electrons), not diamagnetic, so an unintuitive distribution of electrons must exist to induce diamagnetism.

The three logical possibilities are:

1) Low-spin Fe2+ binds to high-energy singlet oxygen. Both low-spin iron and singlet oxygen are diamagnetic.

2) High-spin Fe3+ binds to .O2- (the superoxide ion) and antiferromagnetism oppositely aligns the two unpaired electons, giving diamagnetic properties.

3) Low-spin Fe4+ binds to O22-. Both are diamagnetic.
As discussed above, when oxygen binds to the iron center it causes contraction of the iron atom, and causes it to move back into the center of the porphyrin ring plane (see moving diagram). At the same time, the porphyrin ring plane itself is pushed away from the oxygen and toward the imidizole side chain of the histidine residue interacting at the other pole of the iron. The interaction here forces the ring plane sideways toward the outside of the tetramer, and also induces a strain on the protein helix containing the histidine, as it moves nearer the iron. This causes a tug on this peptide strand which tends to open up heme units in the remainder of the molecule, so that there is more room for oxygen to bind at their heme sites.

In the tetrameric form of normal adult hemoglobin, the binding of oxygen is thus a cooperative process. The binding affinity of hemoglobin for oxygen is increased by the oxygen saturation of the molecule, with the first oxygens bound influencing the shape of the binding sites for the next oxygens, in a way favorable for binding. This positive cooperative binding is achieved through steric conformational changes of the hemoglobin protein complex as discussed above, i.e. when one subunit protein in hemoglobin becomes oxygenated, this induces a conformational or structural change in the whole complex, causing the other subunits to gain an increased affinity for oxygen. As a consequence, the oxygen binding curve of hemoglobin is sigmoidal, or S-shaped, as opposed to the normal hyperbolic curve associated with noncooperative binding.

Hemoglobin's oxygen-binding capacity is decreased in the presence of carbon monoxide because both gases compete for the same binding sites on hemoglobin, carbon monoxide binding preferentially in place of oxygen. Carbon dioxide occupies a different binding site on the hemoglobin. Through the enzyme carbonic anhydrase, carbon dioxide reacts with water to give carbonic acid, which decomposes into bicarbonate and protons:

CO2 + H2O → H2CO3 → HCO3- + H+